D004799D08Enzymes, Coenzymes, and Enzyme InhibitorsEnzymes, Coenzymes, and Enzyme Inhibitors (vertaling onbekend)Biological catalysts, their cofactors, and inhibitors.D003067D08.176CoenzymesCoenzymes (vertaling onbekend)Substances that are necessary for the action or enhancement of action of an enzyme. Many vitamins are coenzymes.D001708D08.176.090BiopterinBiopterin (vertaling onbekend)A natural product that has been considered as a growth factor for some insects.D019798D08.176.090.500NeopterinNeopterin (vertaling onbekend)A pteridine derivative present in body fluids; elevated levels result from immune system activation, malignant disease, allograft rejection, and viral infections. (From Stedman, 26th ed) Neopterin also serves as a precursor in the biosynthesis of biopteriD001710D08.176.096BiotinBiotin (vertaling onbekend)A water-soluble, enzyme co-factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk.D003038D08.176.175CobamidesCobamides (vertaling onbekend)blaD003065D08.176.211Coenzyme ACoenzyme A (vertaling onbekend)blaD000214D08.176.211.300Acyl Coenzyme AAcyl Coenzyme A (vertaling onbekend)S-Acyl coenzyme A. Fatty acid coenzyme A derivatives that are involved in the biosynthesis and oxidation of fatty acids as well as in ceramide formation.D000105D08.176.211.300.075Acetyl Coenzyme AAcetyl Coenzyme A (vertaling onbekend)Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.D008316D08.176.211.300.500Malonyl Coenzyme AMalonyl Coenzyme A (vertaling onbekend)A coenzyme A derivative which plays a key role in the fatty acid synthesis in the cytoplasmic and microsomal systems.D010171D08.176.211.300.700Palmitoyl Coenzyme APalmitoyl Coenzyme A (vertaling onbekend)A fatty acid coenzyme derivative which plays a key role in fatty acid oxidation and biosynthesis.D005182D08.176.315Flavin-Adenine DinucleotideFlavin-Adenine Dinucleotide (vertaling onbekend)A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)D005486D08.176.360FMNFMN (vertaling onbekend)Riboflavin 5'-(dihydrogen phosphate). A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.D009243D08.176.589NADNAD (vertaling onbekend)A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by beingD009249D08.176.625NADPNADP (vertaling onbekend)Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number D011732D08.176.740Pyridoxal PhosphatePyridoxal Phosphate (vertaling onbekend)This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently convertD013763D08.176.840TetrahydrofolatesTetrahydrofolates (vertaling onbekend)blaD005575D08.176.840.300FormyltetrahydrofolatesFormyltetrahydrofolates (vertaling onbekend)Tetrahydrofolates which are substituted by a formyl group at either the nitrogen atom in the 5 position or the nitrogen atom in the 10 position. N(5)-Formyltetrahydrofolate is leukovorin (citrovorum factor) while N(10)-formyltetrahydrofolate is an active D013835D08.176.878Thiamine PyrophosphateThiamine Pyrophosphate (vertaling onbekend)The coenzyme form of vitamin B1 (THIAMINE), present in many animal tissues. It is a required intermediate in the PYRUVATE DEHYDROGENASE COMPLEX and the KETOGLUTARATE DEHYDROGENASE COMPLEX.D008063D08.176.906Thioctic AcidThioctic Acid (vertaling onbekend)A vitamin-like antioxidant that acts as a free-radical scavenger.D014451D08.176.935UbiquinoneUbiquinone (vertaling onbekend)A lipid-soluble benzoquinone which is involved in electron transport in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals.D003580D08.262CytochromesCytochromes (vertaling onbekend)Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium betweD017936D08.262.175Cytochrome aCytochrome a (vertaling onbekend)Cytochromes (electron-transporting proteins) in which the heme prosthetic group is heme a, i.e., the iron chelate of cytoporphyrin IX. (From Enzyme Nomenclature, 1992, p539)D003576D08.262.175.285Cytochrome-c OxidaseCytochrome-c Oxidase (vertaling onbekend)The terminal oxidase of the respiratory chain. It collects electrons that are transferred from reduced CYTOCHROME C and donates them to molecular oxygen, which is then reduced to water. It is composed of CYTOCHROME A and CYTOCHROME B, two copper atoms, anD003573D08.262.200Cytochrome bCytochrome b (vertaling onbekend)Cytochromes (electron-transporting proteins) with protoheme or a related heme as the prosthetic group. The prosthetic group is not covalently bound to the protein moiety.D015786D08.262.200.220Cytochrome b5Cytochrome b5 (vertaling onbekend)A cytochrome occurring in the endoplasmic reticulum that acts as an intermediate electron carrier in some reactions catalyzed by mixed function oxidases, e.g., fatty acid desaturation. It further activates molecular oxygen for an attack on the substrate. D003574D08.262.286Cytochrome cCytochrome c (vertaling onbekend)A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539)D003575D08.262.286.370Cytochrome c1Cytochrome c1 (vertaling onbekend)The 30-kD membrane-bound c-type protein of mitochondria that functions as an electron donor to CYTOCHROME C in the mitochondrial and bacterial respiratory chain. (From Enzyme Nomenclature, 1992, p545)D017937D08.262.300Cytochrome dCytochrome d (vertaling onbekend)Cytochromes (electron-transporting proteins) with a tetrapyrrolic chelate of iron as a prosthetic group in which the degree of conjugation of double bonds is less than in porphyrin. (From Enzyme Nomenclature, 1992, p539)D003577D08.262.453Cytochrome P-450Cytochrome P-450 (vertaling onbekend)Isozymes which are key components of the mixed-function oxidase system responsible for the biotransformation of many foreign compounds to mutagens and carcinogens. Most mammals have several distantly related phenobarbital-inducible gene subfamilies. EC 1.D001141D08.262.453.025AromataseAromatase (vertaling onbekend)An enzyme which converts androgens to estrogens by desaturating ring A of the steroid. This enzyme complex is located in the endoplasmic reticulum of estrogen-producing cells including ovaries, placenta, testicular Sertoli and Leydig cells, adipose, and bD001189D08.262.453.040Aryl Hydrocarbon HydroxylasesAryl Hydrocarbon Hydroxylases (vertaling onbekend)A group of cytochrome P-450 (heme-thiolate) proteins which utilize reduced flavin or flavoprotein as one donor and incorporate one atom of oxygen. They act on many aromatic compounds. They are a component part of the mixed-function oxidase system and are D000815D08.262.453.040.050Aniline HydroxylaseAniline Hydroxylase (vertaling onbekend)A drug-metabolizing, cytochrome P-450 enzyme which catalyzes the hydroxylation of aniline to hydroxyaniline in the presence of reduced flavoprotein and molecular oxygen. EC 1.14.14.-.D001579D08.262.453.040.110Benzopyrene HydroxylaseBenzopyrene Hydroxylase (vertaling onbekend)A drug-metabolizing, cytochrome P-448 (P-450) enzyme which catalyzes the hydroxylation of benzopyrene to 3-hydroxybenzopyrene in the presence of reduced flavoprotein and molecular oxygen. Also acts on certain anthracene derivatives. An aspect of EC 1.14.1D019475D08.262.453.085Camphor 5-MonooxygenaseCamphor 5-Monooxygenase (vertaling onbekend)A monooxygenase heme-thiolate (cytochrome P-450) with camphor bound at the active site. It acts as the terminal monooxygenase in the d-camphor monooxygenase system. Under anaerobic conditions, this enzyme reduces the polyhalogenated compounds bound at theD002790D08.262.453.100Cholesterol 7 alpha-MonooxygenaseCholesterol 7 alpha-Monooxygenase (vertaling onbekend)An enzyme that catalyzes the hydroxylation of cholesterol to cholest-5-en-3 beta,7 alpha-diol. EC 1.14.13.17.D002786D08.262.453.110Cholesterol Monooxygenase (Side-Chain-Cleaving)Cholesterol Monooxygenase (Side-Chain-Cleaving) (vertaling onbekend)Multi-enzyme complex required for the conversion of cholesterol to adrenal cortex hormones. It releases methylpentanoate or isocaproaldehyde and pregnenolone. The complex contains cytochrome P-450, a flavoprotein, a non-heme iron protein, and NADPH. EC 1.D019363D08.262.453.120Cytochrome P-450 CYP1A1Cytochrome P-450 CYP1A1 (vertaling onbekend)A cytochrome P-450 enzyme capable of activating procarcinogenic polycyclic hydrocarbons and halogenated aromatic hydrocarbons into mutagenic compounds. Ethoxyresorufin acts as a substrate for CYP1A1 and measurement of ethoxyresorufin O-deethylase providesD019388D08.262.453.130Cytochrome P-450 CYP1A2Cytochrome P-450 CYP1A2 (vertaling onbekend)A polycyclic aromatic hydrocarbon-inducible cytochrome which is of significant clinical interest due to the large number of drug interactions associated with induction and inhibition of theophylline. Caffeine is considered to be a model substrate for thisD019362D08.262.453.140Cytochrome P-450 CYP2B1Cytochrome P-450 CYP2B1 (vertaling onbekend)A major cytochrome P-450 enzyme which is inducible by phenobarbital in both the liver and small intestine. It is active in the metabolism of compounds like pentoxyresorufin, testosterone, and androstenedione. CYP2B1 also mediates the activation of cyclophD019389D08.262.453.160Cytochrome P-450 CYP2D6Cytochrome P-450 CYP2D6 (vertaling onbekend)A polymorphic enzyme that catalyzes the hydroxylation of debrisoquine. It also metabolizes several antidepressants and neuroleptics. This enzyme is deficient in up to 10 percent of the population. (Psychopharmacol Bull 1995; 31(2): 327-331) EC 1.14.99.-.D019392D08.262.453.170Cytochrome P-450 CYP2E1Cytochrome P-450 CYP2E1 (vertaling onbekend)A polymorphic enzyme that activates carcinogenic N-nitrosamines, benzene, urethane, and other low molecular weight compounds. It is inducible by ethanol and metabilizes alcohol. Experimentally, it is used to study the effects of ethanol usage and withdrawD019405D08.262.453.180Cytochrome P-450 CYP11B2Cytochrome P-450 CYP11B2 (vertaling onbekend)A multifunctional enzyme that catalyzes the conversion of corticosterone to 18-hydroxycorticosterone and the subsequent conversion of 18-hydroxycorticosterone to aldosterone. EC 1.14.99.-.D015090D08.262.453.40025-Hydroxycholecalciferol 1-Hydroxylase25-Hydroxycholecalciferol 1-Hydroxylase (vertaling onbekend)An enzyme that catalyzes the formation of 1,25-dihydroxycholecalciferol from 25-hydroxycholecalciferol. The reaction requires oxygen, magnesium, and NAD(P)H. EC 1.14.13.13.D013254D08.262.453.800Steroid 17 alpha-MonooxygenaseSteroid 17 alpha-Monooxygenase (vertaling onbekend)A steroid hydroxylase system found in the microsomal membrane of the steroid-hormone producing tissues. It catalyzes the 17-hydroxylation of steroids, such as progesterone or pregnenolone in the presence of NADPH and molecular oxygen. This is an importantD013252D08.262.453.810Steroid 11 beta-MonooxygenaseSteroid 11 beta-Monooxygenase (vertaling onbekend)A steroid hydroxylase system found in adrenal tissues. It catalyzes the 11-hydroxylation of steroids in the presence of molecular oxygen and consists of an NADPH-specific flavoprotein, a non-heme iron protein, and cytochrome P-450. Its deficiency is a cauD013253D08.262.453.820Steroid 12-MonooxygenaseSteroid 12-Monooxygenase (vertaling onbekend)A steroid hydroxylase found in liver microsomes. It catalyzes the 12-hydroxylation of steroids in the presence of NADPH, cytochrome P-450, and molecular oxygen. It is an important enzyme in the synthesis of cholic acid from cholesterol in the liver. EC 1.D013255D08.262.453.830Steroid 21-MonooxygenaseSteroid 21-Monooxygenase (vertaling onbekend)A steroid hydroxylase system found in adrenal cortex microsomes. It catalyzes the 21-hydroxylation of corticosteroids and shows a requirement for NADPH and molecular oxygen. Its deficiency is a cause of adrenogenital syndrome. EC 1.14.99.10.D004791D08.373Enzyme InhibitorsEnzyme Inhibitors (vertaling onbekend)Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.D002257D08.373.220Carbonic Anhydrase InhibitorsCarbonic Anhydrase Inhibitors (vertaling onbekend)A class of compounds that reduces the secretion of H+ ions by the proximal kidney tubule through inhibition of CARBONIC ANHYDRASES.D002800D08.373.275Cholinesterase InhibitorsCholinesterase Inhibitors (vertaling onbekend)Drugs that inhibit cholinesterases. The neurotransmitter ACETYLCHOLINE is rapidly hydrolyzed, and thereby inactivated, by cholinesterases. When cholinesterases are inhibited, the action of endogenously released acetylcholine at cholinergic synapses is potD016861D08.373.310Cyclooxygenase InhibitorsCyclooxygenase Inhibitors (vertaling onbekend)Compounds or agents that combine with cyclooxygenase (PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE) and thereby prevent its substrate-enzyme combination with arachidonic acid and the formation of eicosanoids, prostaglandins, and thromboxanes.D005493D08.373.350Folic Acid AntagonistsFolic Acid Antagonists (vertaling onbekend)Inhibitors of the enzyme, dihydrofolate reductase (TETRAHYDROFOLATE DEHYDROGENASE), which converts dihydrofolate (FH2) to tetrahydrofolate (FH4). They are frequently used in cancer chemotherapy. (From AMA, Drug Evaluations Annual, 1994, p2033)D019161D08.373.370Hydroxymethylglutaryl-CoA Reductase InhibitorsHydroxymethylglutaryl-CoA Reductase Inhibitors (vertaling onbekend)Compounds that inhibit HMG-CoA reductases. They have been shown to directly lower cholesterol synthesis.D019429D08.373.375Integrase InhibitorsIntegrase Inhibitors (vertaling onbekend)Compounds which inhibit or antagonize biosynthesis or actions of integrase.D019428D08.373.375.400HIV Integrase InhibitorsHIV Integrase Inhibitors (vertaling onbekend)Inhibitors of HIV INTEGRASE, an enzyme required for integration of viral DNA into cellular DNA.D016859D08.373.390Lipoxygenase InhibitorsLipoxygenase Inhibitors (vertaling onbekend)Compounds or agents that combine with lipoxygenase and thereby prevent its substrate-enzyme combination with arachidonic acid and the formation of the eicosanoid products hydroxyeicosatetraenoic acid and various leukotrienes.D008996D08.373.616Monoamine Oxidase InhibitorsMonoamine Oxidase Inhibitors (vertaling onbekend)A chemically heterogeneous group of drugs that have in common the ability to block oxidative deamination of naturally occurring monoamines. (From Gilman, et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 8th ed, p414)D019384D08.373.675Nucleic Acid Synthesis InhibitorsNucleic Acid Synthesis Inhibitors (vertaling onbekend)Compounds that inhibit cell production of DNA or RNA.D018894D08.373.675.850Reverse Transcriptase InhibitorsReverse Transcriptase Inhibitors (vertaling onbekend)Inhibitors of reverse transcriptase (RNA-DIRECTED DNA POLYMERASE), an enzyme that synthesizes DNA on an RNA template.D010726D08.373.735Phosphodiesterase InhibitorsPhosphodiesterase Inhibitors (vertaling onbekend)Compounds which inhibit or antagonize the biosynthesis or actions of phosphodiesterases.D011480D08.373.745Protease InhibitorsProtease Inhibitors (vertaling onbekend)Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).D000806D08.373.745.085Angiotensin-Converting Enzyme InhibitorsAngiotensin-Converting Enzyme Inhibitors (vertaling onbekend)A class of drugs whose main indications are the treatment of hypertension and heart failure. They exert their hemodynamic effect mainly by inhibiting the renin-angiotensin system. They also modulate sympathetic nervous system activity and increase prostagD015853D08.373.745.325Cysteine Proteinase InhibitorsCysteine Proteinase Inhibitors (vertaling onbekend)Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.D017320D08.373.745.420HIV Protease InhibitorsHIV Protease Inhibitors (vertaling onbekend)Inhibitors of HIV PROTEASE, an enzyme required for production of proteins needed for viral assembly.D015842D08.373.745.800Serine Proteinase InhibitorsSerine Proteinase Inhibitors (vertaling onbekend)Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.D014361D08.373.745.800.900Trypsin InhibitorsTrypsin Inhibitors (vertaling onbekend)Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.D019714D08.373.745.850Tissue Inhibitor of MetalloproteinasesTissue Inhibitor of Metalloproteinases (vertaling onbekend)A family of secreted proteins (TIMP-1; TIMP-2; and TIMP-3) that play a crucial role in regulating the activity of the secreted METALLOENDOPEPTIDASES (COLLAGENASES; stromelysins, GELATINASES). Of the three characterized, only TIMP-1 and TIMP-2 appear to haD019715D08.373.745.850.450Tissue-Inhibitor of Metalloproteinase-1Tissue-Inhibitor of Metalloproteinase-1 (vertaling onbekend)A member of the family of TISSUE INHIBITOR OF METALLOPROTEINASES. It is a N-glycosylated protein, molecular weight 28 kD, produced by a vast range of cell types and found in a variety of tissues and body fluids. It has been shown to suppress metastasis anD019716D08.373.745.850.500Tissue Inhibitor-of Metalloproteinase-2Tissue Inhibitor-of Metalloproteinase-2 (vertaling onbekend)A member of the family of TISSUE INHIBITOR OF METALLOPROTEINASES. It is a 21 kD nonglycosylated protein found in tissue fluid and is secreted as a complex with progelatinase A by human fibroblast and uncomplexed from alveolar macrophages. An overexpressioD019717D08.373.745.850.550Tissue Inhibitor of-Metalloproteinase-3Tissue Inhibitor of-Metalloproteinase-3 (vertaling onbekend)A member of the family of TISSUE INHIBITOR OF METALLOPROTEINASES. It is a 21 kD, nonglycosylated protein. TIMP-3 does not show a high degree of structural similarity unlike TIMP-1 and TIMP-2 which are structurally similar. However, it does possess a high D011500D08.373.760Protein Synthesis InhibitorsProtein Synthesis Inhibitors (vertaling onbekend)Compounds which inhibit the synthesis of proteins. They are usually antibiotics or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the the A site of ribosomes, the misreading of the geneticD014475D08.373.936Uncoupling AgentsUncoupling Agents (vertaling onbekend)Chemical agents that uncouple oxidation from phosphorylation in the metabolic cycle so that ATP synthesis does not occur. Included here are those IONOPHORES that disrupt electron transfer by short-circuiting the proton gradient across mitochondrial membraD004792D08.444Enzyme PrecursorsEnzyme Precursors (vertaling onbekend)Physiologically inactive substances that can be converted to active enzymes.D002919D08.444.184ChymotrypsinogenChymotrypsinogen (vertaling onbekend)blaD011415D08.444.200Complement Factor BComplement Factor B (vertaling onbekend)A glycine-rich, heat-labile beta-glycoprotein found in blood. It is a proactivator of complement 3 in the alternate pathway of complement activation. Factor B is converted by Factor D to COMPLEMENT 3 CONVERTASE. EC 3.4.21.47.D010435D08.444.509PepsinogensPepsinogens (vertaling onbekend)Proenzymes secreted by chief cells, mucous neck cells, and pyloric gland cells, which are converted into pepsin in the presence of gastric acid or pepsin itself. (Dorland, 28th ed) In humans there are 2 related pepsinogen systems: PEPSINOGEN A (formerly pD020116D08.444.509.700Pepsinogen APepsinogen A (vertaling onbekend)This is one of 2 related pepsinogen systems in humans and is also known as pepsinogen. (The other is PEPSINOGEN C.) This includes isozymogens Pg1-Pg5 (pepsinogens 1-5, group I or products of PGA1-PGA5 genes). This is the main pepsinogen found in urine.D020115D08.444.509.725Pepsinogen CPepsinogen C (vertaling onbekend)This is one of the 2 related pepsinogen systems in humans. It is found in prostate and seminal fluid whereas PEPSINOGEN A is not.D010958D08.444.610PlasminogenPlasminogen (vertaling onbekend)Precursor of fibrinolysin (plasmin). It is a single-chain beta-globulin of molecular weight 80-90,000 found mostly in association with fibrinogen in plasma; plasminogen activators change it to fibrinolysin. It is used in wound debriding and has been invesD011486D08.444.705Protein CProtein C (vertaling onbekend)A vitamin-K dependent zymogen present in the blood, which, upon activation by thrombin and thrombomodulin exerts anticoagulant properties by inactivating factors Va and VIIIa at the rate-limiting steps of thrombin formation.D011516D08.444.709ProthrombinProthrombin (vertaling onbekend)A plasma protein that is the inactive precursor of thrombin. It is converted to thrombin by a prothrombin activator complex consisting of factor Xa, factor V, phospholipid, and calcium ions. Deficiency of prothrombin leads to hypoprothrombinemia.D014362D08.444.885TrypsinogenTrypsinogen (vertaling onbekend)The inactive proenzyme of trypsin secreted by the pancreas, activated in the duodenum via cleavage by enteropeptidase. (Stedman, 25th ed)D004793D08.515Enzyme ReactivatorsEnzyme Reactivators (vertaling onbekend)Compounds which restore enzymatic activity by removing an inhibitory group bound to the reactive site of the enzyme.D002801D08.515.347Cholinesterase ReactivatorsCholinesterase Reactivators (vertaling onbekend)Drugs used to reverse the inactivation of cholinesterase caused by organophosphates or sulfonates. They are an important component of therapy in agricultural, industrial, and military poisonings by organophosphates and sulfonates.D004798D08.586EnzymesEnzymes (vertaling onbekend)Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however catalytic RNA (RNA, CATALYTIC) and catalytic DNA (DNA, CATALYTIC) molecules have also been identified.D015280D08.586.150DNA Restriction-Modification EnzymesDNA Restriction-Modification Enzymes (vertaling onbekend)Systems consisting of two enzymes, a modification methylase and a restriction endonuclease. They are closely related in their specificity and protect the DNA of a given bacterial species. The methylase adds methyl groups to adenine or cytosine residues inD015254D08.586.150.240DNA Modification MethylasesDNA Modification Methylases (vertaling onbekend)Enzymes that are part of the restriction-modification systems. They are responsible for producing a species-characteristic methylation pattern, on either adenine or cytosine residues, in a specific short base sequence in the host cell's own DNA. ThisD004262D08.586.150.280DNA Restriction EnzymesDNA Restriction Enzymes (vertaling onbekend)Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded D015253D08.586.150.280.250Deoxyribonucleases, Type I Site-SpecificDeoxyribonucleases, Type I Site-Specific (vertaling onbekend)Enzyme systems containing three different subunits and requiring ATP, S-adenosylmethionine, and magnesium for endonucleolytic activity to give random double-stranded fragments with terminal 5'-phosphates. They function also as DNA-dependent ATPases aD015252D08.586.150.280.260Deoxyribonucleases, Type II Site-SpecificDeoxyribonucleases, Type II Site-Specific (vertaling onbekend)Enzyme systems containing a single subunit and requiring only magnesium for endonucleolytic activity. The corresponding modification methylases are separate enzymes. The systems recognize specific short DNA sequences and cleave either within, or at a shorD015245D08.586.150.280.260.240Deoxyribonuclease BamHIDeoxyribonuclease BamHI (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence G/GATCC at the slash. BamHI is from Bacillus amyloliquefaciens N. Numerous isoschizomers have been identified. EC 3.1.21.-.D015246D08.586.150.280.260.300Deoxyribonuclease EcoRIDeoxyribonuclease EcoRI (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence G/AATTC at the slash. EcoRI is from E coliRY13. Several isoschizomers have been identified. EC 3.1.21.-.D015247D08.586.150.280.260.400Deoxyribonuclease HindIIIDeoxyribonuclease HindIII (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence A/AGCTT at the slash. HindIII is from Haemophilus influenzae R(d). Numerous isoschizomers have been identified. EC 3.1.21.-.D019003D08.586.150.280.260.420Deoxyribonuclease HpaIIDeoxyribonuclease HpaII (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequences C/CGG and GGC/C at the slash. HpaII is from Haemophilus parainfluenzae. Several isoschizomers have been identified. EC 3.1.21.-.D015263D08.586.150.280.270Deoxyribonucleases, Type III Site-SpecificDeoxyribonucleases, Type III Site-Specific (vertaling onbekend)Enzyme systems composed of two subunits and requiring ATP and magnesium for endonucleolytic activity; they do not function as ATPases. They exist as complexes with modification methylases of similar specificity listed under EC 2.1.1.72 or EC 2.1.1.73. TheD021881D08.586.165DNA, CatalyticDNA, Catalytic (vertaling onbekend)Molecules of DNA that possess enzymatic activity.D004800D08.586.180Enzymes, ImmobilizedEnzymes, Immobilized (vertaling onbekend)Enzymes which are immobilized on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilized enzymes have found wide application in the industrial, medD020035D08.586.255HoloenzymesHoloenzymes (vertaling onbekend)Catalytically active enzymes that are formed by the combination of an apoenzyme (APOENZYMES) and its appropriate cofactors and prosthetic groups.D006867D08.586.277HydrolasesHydrolases (vertaling onbekend)Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphaD017766D08.586.277.040Acid Anhydride HydrolasesAcid Anhydride Hydrolases (vertaling onbekend)A group of enzymes that catalyze the hydrolysis of diphosphate bonds in compounds such as nucleoside di- and tri-phosphates, and sulfonyl-containing anhydrides such as adenylylsulfate. (Enzyme Nomenclature, 1992) EC 3.6.D000251D08.586.277.040.025AdenosinetriphosphataseAdenosinetriphosphatase (vertaling onbekend)A group of enzymes which catalyze the hydrolysis of ATP coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA. EC 3.6.1.3.D017301D08.586.277.040.025.095Ca(2+) Mg(2+)-ATPaseCa(2+) Mg(2+)-ATPase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of ATP and is activated by millimolar concentrations of either Ca(2+) or Mg(2+). Unlike CA(2+)-TRANSPORTING ATPASE it does not require the second divalent cation for its activity, and is not sensitive to orthovanadaD000252D08.586.277.040.025.125Ca(2+)-Transporting ATPaseCa(2+)-Transporting ATPase (vertaling onbekend)An enzyme found in the sarcoplasmic reticulum vesicle membrane. During the relaxation of skeletal muscles and muscle rich in mitochondria, this enzyme catalyzes the active transport of calcium into the sarcoplasmic reticulum vesicles from the sarcoplasm. D004398D08.586.277.040.025.150Dynein ATPaseDynein ATPase (vertaling onbekend)A structural protein which forms the arms on the microtubule doublets of cilia and flagella. In the presence of divalent cations, dynein catalyzes the hydrolysis of ATP. This hydrolysis plays an important functional role in the motility process. EC 3.6.1.D017506D08.586.277.040.025.300H(+)-K(+)-Exchanging ATPaseH(+)-K(+)-Exchanging ATPase (vertaling onbekend)An enzyme isolated from the gastric mucosa that catalyzes the hydrolysis of ATP coupled with the exchange of hydrogen and potassium ions across the cell wall. EC 3.6.1.36.D006180D08.586.277.040.025.325Proton-Translocating ATPasesProton-Translocating ATPases (vertaling onbekend)Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane.D025243D08.586.277.040.025.325.249Bacterial Proton-Translocating ATPasesBacterial Proton-Translocating ATPases (vertaling onbekend)Membrane-bound proton-translocating ATPases that serve two important physiological functions in bacteria. One function is to generate ADENOSINE TRIPHOSPHATE by utilizing the energy provided by an electrochemical gradient of protons across the cellular memD025222D08.586.277.040.025.325.500Chloroplast Proton-Translocating ATPasesChloroplast Proton-Translocating ATPases (vertaling onbekend)Proton-translocating ATPases which produce ADENOSINE TRIPHOSPHATE in plants. They derive energy from light-driven reactions that develop high concentrations of protons within the membranous cisternae (THYLAKOIDS) of the CHLOROPLASTS.D025261D08.586.277.040.025.325.750Mitochondrial Proton-Translocating ATPasesMitochondrial Proton-Translocating ATPases (vertaling onbekend)Proton-translocating ATPases responsible for ADENOSINE TRIPHOSPHATE synthesis in the MITOCHONDRIA. They derive energy from the respiratory chain-driven reactions that develop high concentrations of protons within the intermembranous space of the mitochondD025262D08.586.277.040.025.325.875Vacuolar Proton-Translocating ATPasesVacuolar Proton-Translocating ATPases (vertaling onbekend)Proton-translocating ATPases that are involved in acidification of a variety of intracellular compartments.D016547D08.586.277.040.025.450KinesinKinesin (vertaling onbekend)A microtubule-associated mechanical adenosine triphosphatase, that uses the energy of ATP hydrolysis to move organelles along microtubules toward the plus end of the microtubule. The protein is found in squid axoplasm, optic lobes, and in bovine brain. BoD009218D08.586.277.040.025.525MyosinsMyosins (vertaling onbekend)A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyse MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chainsD024461D08.586.277.040.025.525.500Myosin Type IMyosin Type I (vertaling onbekend)A subclass of myosins found generally associated with actin-rich membrane structures such as filopodia. Members of the myosin type I family are ubiquitously expressed in eukaryotes. The heavy chains of myosin type I lack coiled-coil forming sequences in tD024462D08.586.277.040.025.525.750Myosin Type IIMyosin Type II (vertaling onbekend)The subfamily of myosin proteins that are commonly found in muscle fibers. Myosin II is also involved a diverse array of cellular functions including cell division, transport within the GOLGI APPARATUS, and maintaining MICROVILLI structure.D024722D08.586.277.040.025.525.750.124Cardiac MyosinsCardiac Myosins (vertaling onbekend)Myosin type II isoforms found in cardiac muscle.D024743D08.586.277.040.025.525.750.124.249Atrial MyosinsAtrial Myosins (vertaling onbekend)Myosin type II isoforms specifically found in the atrial muscle of the heart.D024723D08.586.277.040.025.525.750.124.500Ventricular MyosinsVentricular Myosins (vertaling onbekend)Myosin type II isoforms specifically found in the ventricular muscle of the heart.D024507D08.586.277.040.025.525.750.374Nonmuscle Myosin Type IIANonmuscle Myosin Type IIA (vertaling onbekend)A nonmuscle isoform of myosin type II found predominantly in platelets, lymphocytes, neutrophils and brush border enterocytes.D024501D08.586.277.040.025.525.750.500Nonmuscle Myosin Type IIBNonmuscle Myosin Type IIB (vertaling onbekend)A nonmuscle isoform of myosin type II found predominantly in neuronal tissue.D024744D08.586.277.040.025.525.750.750Skeletal Muscle MyosinsSkeletal Muscle Myosins (vertaling onbekend)Myosin type II isoforms found in skeletal muscle.D024745D08.586.277.040.025.525.750.875Smooth Muscle MyosinsSmooth Muscle Myosins (vertaling onbekend)Myosin type II isoforms found in smooth muscle.D025102D08.586.277.040.025.525.812Myosin Type IIIMyosin Type III (vertaling onbekend)A subclass of myosins originally found in the photoreceptor of DROSOPHILA. The heavy chains can occur as two alternatively spliced isoforms of 132 and 174 KD. The amino terminal of myosin type III is highly unusual in that it contains a protein kinase domD025121D08.586.277.040.025.525.843Myosin Type IVMyosin Type IV (vertaling onbekend)A subclass of myosin found in ACANTHAMOEBA. It is a non-filamentous myosin containing a single 180 KD myosin heavy chain.D024701D08.586.277.040.025.525.875Myosin Type VMyosin Type V (vertaling onbekend)A subclass of myosin involved in organelle transport and membrane targeting. It is abundantly found in nervous tissue and neurosecretory cells. The heavy chains of myosin V contain unusually long neck domains that are believed to aid in translocating molD000254D08.586.277.040.025.600Na(+)-K(+)-Exchanging ATPaseNa(+)-K(+)-Exchanging ATPase (vertaling onbekend)An enzyme that catalyzes the active transport system of sodium and potassium ions across the cell wall. Sodium and potassium ions are closely coupled with membrane ATPase which undergoes phosphorylation and dephosphorylation, thereby providing energy for D001081D08.586.277.040.050ApyraseApyrase (vertaling onbekend)A calcium-activated enzyme that catalyzes the hydrolysis of ATP to yield AMP and orthophosphate. It can also act on ADP and other nucleoside triphosphates and diphosphates. EC 3.6.1.5.D020558D08.586.277.040.330GTP PhosphohydrolasesGTP Phosphohydrolases (vertaling onbekend)Enzymes that hydrolyze GTP to GDP. EC 3.6.1.-.D019204D08.586.277.040.330.300GTP-Binding ProteinsGTP-Binding Proteins (vertaling onbekend)Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control theD020963D08.586.277.040.330.300.100GTP Phosphohydrolase-Linked Elongation FactorsGTP Phosphohydrolase-Linked Elongation Factors (vertaling onbekend)Factors that utilize energy from the hydrolysis of GTP to GDP for peptide chain elongation. EC 3.6.1.-.D020653D08.586.277.040.330.300.100.200Peptide Elongation Factor GPeptide Elongation Factor G (vertaling onbekend)Peptide Elongation Factor G catalyzes the translocation of peptidyl-tRNA from the A to the P site of bacterial ribosomes by a process linked to hydrolysis of GTP to GDP.D010444D08.586.277.040.330.300.100.700Peptide Elongation Factor TuPeptide Elongation Factor Tu (vertaling onbekend)A protein found in bacteria and eukaryotic mitochondria which delivers aminoacyl-tRNA's to the A site of the ribosome. The aminoacyl-tRNA is first bound to a complex of elongation factor Tu containing a molecule of bound GTP. The resulting complex isD020648D08.586.277.040.330.300.100.800Peptide Elongation Factor 1Peptide Elongation Factor 1 (vertaling onbekend)Peptide elongation factor 1 is a multisubunit protein that is responsible for the GTP-dependent binding of aminoacyl-tRNAs to eukaryotic ribosomes. The alpha subunit (EF-1alpha) binds aminoacyl-tRNA and transfers it to the ribosome in a process linked to D020652D08.586.277.040.330.300.100.850Peptide Elongation Factor 2Peptide Elongation Factor 2 (vertaling onbekend)Peptide Elongation Factor 2 catalyzes the translocation of peptidyl-tRNA from the A site to the P site of eukaryotic ribosomes by a process linked to the hydrolysis of GTP to GDP.D020962D08.586.277.040.330.300.200Heterotrimeric GTP-Binding ProteinsHeterotrimeric GTP-Binding Proteins (vertaling onbekend)GTP-BINDING PROTEINS that contain three non-identical subunits. They are found associated with members of the seven transmembrane domain superfamily of G-protein coupled receptors. The G-alpha subunit acts as a signal transduction molecule when it binds GD019206D08.586.277.040.330.300.200.445G-Protein, Inhibitory GiG-Protein, Inhibitory Gi (vertaling onbekend)A heterotrimeric GTP-binding protein that inhibits adenylate cyclase and activates potassium channels. EC 3.6.1.-.D019205D08.586.277.040.330.300.200.460G-Protein, Stimulatory GsG-Protein, Stimulatory Gs (vertaling onbekend)A heterotrimeric GTP-binding protein that activates adenylate cyclase. EC 3.6.1.-.D015293D08.586.277.040.330.300.200.800TransducinTransducin (vertaling onbekend)A heterotrimeric GTP-binding protein that mediates the light activation signal from photolyzed rhodopsin to cyclic GMP phosphodiesterase and is pivotal in the visual excitation process. Activation of rhodopsin on the outer membrane of rod and cone cells cD020559D08.586.277.040.330.300.400Monomeric GTP-Binding ProteinsMonomeric GTP-Binding Proteins (vertaling onbekend)A class of monomeric, low molecular weight (20-25 kDa) GTP-binding proteins that regulate a variety of intracellular processes. The GTP bound form of the protein is active and limited by its inherent GTPase activity, which is controlled by an array of GTPD020727D08.586.277.040.330.300.400.100ADP-Ribosylation FactorsADP-Ribosylation Factors (vertaling onbekend)MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the NAD(P)(+)-ARGININE ADP-RIBOSYLTRANSFERASE of the cholera toxin catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. EC D020823D08.586.277.040.330.300.400.100.100ADP-Ribosylation Factor 1ADP-Ribosylation Factor 1 (vertaling onbekend)ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with organelle membranes in the early secretory pathway. It is a component of COAT PROTEIN COMPLEX I.D020691D08.586.277.040.330.300.400.400rab GTP-Binding Proteinsrab GTP-Binding Proteins (vertaling onbekend)A large family of MONOMERIC GTP-BINDING PROTEINS that play a key role in cellular secretory and endocytic pathways. EC 3.6.1.-.D020761D08.586.277.040.330.300.400.400.025rab1 GTP-Binding Proteinsrab1 GTP-Binding Proteins (vertaling onbekend)A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS and through early Golgi compartments. EC 3.6.1.-.D020693D08.586.277.040.330.300.400.400.050rab2 GTP-Binding Proteinrab2 GTP-Binding Protein (vertaling onbekend)A protein involved in transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS. EC 3.6.1.-.D020692D08.586.277.040.330.300.400.400.100rab3 GTP-Binding Proteinsrab3 GTP-Binding Proteins (vertaling onbekend)A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in calcium-dependent EXOCYTOSIS. EC 3.6.1.-.D020826D08.586.277.040.330.300.400.400.125rab3A GTP-Binding Proteinrab3A GTP-Binding Protein (vertaling onbekend)The most abundant member of the RAB3 GTP-BINDING PROTEINS. It is involved in calcium-dependent EXOCYTOSIS and is localized to neurons and neuroendocrine cells. EC 3.6.1.-D020695D08.586.277.040.330.300.400.400.150rab4 GTP-Binding Proteinsrab4 GTP-Binding Proteins (vertaling onbekend)A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in recycling of proteins such as cell surface receptors from early endosomes to the cell surface. EC 3.6.1.-.D020696D08.586.277.040.330.300.400.400.200rab5 GTP-Binding Proteinsrab5 GTP-Binding Proteins (vertaling onbekend)A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in transport from the cell membrane to early endosomes. EC 3.6.1.-.D020725D08.586.277.040.330.300.400.450ral GTP-Binding Proteinsral GTP-Binding Proteins (vertaling onbekend)A family of ubiquitously expressed MONOMERIC GTP-BINDING PROTEINS that are involved in intracellular signal transduction. EC 3.6.1.-.D020931D08.586.277.040.330.300.400.462ran GTP-Binding Proteinran GTP-Binding Protein (vertaling onbekend)A monomeric GTP-binding protein involved in nucleocytoplasmic transport of proteins into the nucleus and RNA into the cytoplasm. EC 3.6.1.-.D020668D08.586.277.040.330.300.400.475rap GTP-Binding Proteinsrap GTP-Binding Proteins (vertaling onbekend)A family of MONOMERIC GTP-BINDING PROTEINS that are related to RAS PROTEINS. EC 3.6.1.-.D020827D08.586.277.040.330.300.400.475.100rap1 GTP-Binding Proteinsrap1 GTP-Binding Proteins (vertaling onbekend)A genetically related subfamily of RAP GTP-BINDING PROTEINS that share homology with RAS PROTEINS. They bind to Ras effectors but do not activate them, therefore they may antagonize the effects of RAS PROTEINS. EC 3.6.1.-.D018631D08.586.277.040.330.300.400.500ras Proteinsras Proteins (vertaling onbekend)Small, monomeric GTP-binding proteins encoded by ras genes (GENES, RAS). The protooncogene-derived protein (PROTO-ONCOGENE PROTEIN P21(RAS)) plays a role in normal cellular growth, differentiation and development. The oncogene-derived protein (ONCOGENE PRD015689D08.586.277.040.330.300.400.500.300Oncogene Protein p21(ras)Oncogene Protein p21(ras) (vertaling onbekend)Transforming protein encoded by ras oncogenes. Point mutations in the cellular ras gene (c-ras) can also result in a mutant p21 protein that can transform mammalian cells. Oncogene protein p21(ras) has been directly implicated in human neoplasms, perhaps D016283D08.586.277.040.330.300.400.500.600Proto-Oncogene Protein p21(ras)Proto-Oncogene Protein p21(ras) (vertaling onbekend)Cellular protein encoded by the H-ras, K-ras and N-ras genes. The protein has GTPase activity and is involved in signal transduction as a monomeric GTP-Binding protein. Elevated levels of p21 c-ras have been associated with neoplasia. EC 3.6.1.-.D020741D08.586.277.040.330.300.400.700rho GTP-Binding Proteinsrho GTP-Binding Proteins (vertaling onbekend)A large family of MONOMERIC GTP-BINDING PROTEINS that are involved in regulation of actin organization, gene expression and cell cycle progression. EC 3.6.1.-.D020764D08.586.277.040.330.300.400.700.050cdc42 GTP-Binding Proteincdc42 GTP-Binding Protein (vertaling onbekend)A member of the Rho family of MONOMERIC-GTP-BINDING PROTEINS. It is associated with a diverse array of cellular functions including cytoskeletal changes, filopodia formation and transport through the GOLGI APPARATUS. EC 3.6.1.-.D020846D08.586.277.040.330.300.400.700.060cdc42 GTP-Binding Protein, Saccharomyces cerevisiaecdc42 GTP-Binding Protein, Saccharomyces cerevisiae (vertaling onbekend)A member of the Rho family of MONOMERIC GTP-BINDING PROTEINS from SACCHAROMYCES CEREVISIAE. It is involved in morphological events related to the cell cycle. EC 3.6.1.-.D020744D08.586.277.040.330.300.400.700.100rac GTP-Binding Proteinsrac GTP-Binding Proteins (vertaling onbekend)A sub-family of RHO GTP-BINDING PROTEINS that is involved in regulating the organization of cytoskeletal filaments. EC 3.6.1.-.D020830D08.586.277.040.330.300.400.700.110rac1 GTP-Binding Proteinrac1 GTP-Binding Protein (vertaling onbekend)A rac GTP-binding protein involved in regulating actin filaments at the plasma membrane. It controls the development of filopodia and lamellipodia in cells and thereby influences cellular motility and adhesion. It is also involved in activation of NADPH OD020742D08.586.277.040.330.300.400.700.200rhoA GTP-Binding ProteinrhoA GTP-Binding Protein (vertaling onbekend)A RHO GTP-BINDING PROTEIN involved in regulating signal transduction pathways that control assembly of focal adhesions and actin stress fibers. EC 3.6.1.-.D020743D08.586.277.040.330.300.400.700.300rhoB GTP-Binding ProteinrhoB GTP-Binding Protein (vertaling onbekend)A GTP-BINDING PROTEIN involved in regulating a signal transduction pathway that controls assembly of focal adhesions and actin stress fibers. EC 3.6.1.-.D011755D08.586.277.040.600PyrophosphatasesPyrophosphatases (vertaling onbekend)A group of enzymes within the class EC 3.6.1.- that catalyze the hydrolysis of diphosphate bonds, chiefly in nucleoside di- and triphosphates. They may liberate either a mono- or diphosphate. EC 3.6.1.-.D013834D08.586.277.040.600.800Thiamine PyrophosphataseThiamine Pyrophosphatase (vertaling onbekend)An enzyme that hydrolyzes thiamine pyrophosphate to thiamine monophosphate plus inorganic phosphate. EC 3.6.1.-.D013837D08.586.277.040.850Thiamin-TriphosphataseThiamin-Triphosphatase (vertaling onbekend)An enzyme present in nerve tissue. It catalyzes reversibly the formation of thiamine diphosphate and orthophosphate from thiamine triphosphate. EC 3.6.1.28.D000581D08.586.277.087AmidohydrolasesAmidohydrolases (vertaling onbekend)blaD009238D08.586.277.087.030N-Acetylmuramoyl-L-alanine AmidaseN-Acetylmuramoyl-L-alanine Amidase (vertaling onbekend)An autolytic enzyme bound to the surface of bacterial cell walls. It catalyzes the hydrolysis of the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell wall glycopeptides, particularly peptidoglycan. EC 3.5.1.28.D000492D08.586.277.087.060Allophanate HydrolaseAllophanate Hydrolase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of allophanic acid to two molecules of ammonia plus two molecules of "active carbon dioxide". EC 3.5.1.54.D005558D08.586.277.087.100ArylformamidaseArylformamidase (vertaling onbekend)An enzyme that catalyzes the conversion of N-formyl-L-kynurenine and water to formate and L-kynurenine. It also acts on other aromatic formylamines. (Enzyme Nomenclature, 1992) EC 3.5.1.9.D001215D08.586.277.087.116AsparaginaseAsparaginase (vertaling onbekend)A hydrolase enzyme that converts L-asparagine and water to L-aspartate and NH3. EC 3.5.1.1.D001227D08.586.277.087.125AspartylglucosylaminaseAspartylglucosylaminase (vertaling onbekend)An enzyme that catalyzes the conversion of N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine and water to N-acetyl-beta-D-glucosaminylamine and L-aspartate. It acts only on asparagine oligosaccharides containing one amino acid, i.e. the asparagine has freeD001618D08.586.277.087.180beta-Lactamasesbeta-Lactamases (vertaling onbekend)Enzymes found in many bacteria which catalyze the hydrolysis of the amide bond in the beta-lactam ring. Well known antibiotics destroyed by these enzymes are penicillins and cephalosporins. EC 3.5.2.6.D002510D08.586.277.087.180.229CephalosporinaseCephalosporinase (vertaling onbekend)blaD010405D08.586.277.087.180.697PenicillinasePenicillinase (vertaling onbekend)A beta-lactamase preferentially cleaving penicillins. (Dorland, 28th ed) EC 3.5.2.-.D004080D08.586.277.087.280DihydroorotaseDihydroorotase (vertaling onbekend)An enzyme that, in the course of pyrimidine biosynthesis, catalyzes ring closure by removal of water from N-carbamoylaspartate to yield dihydro-orotic acid. EC 3.5.2.3.D005972D08.586.277.087.483GlutaminaseGlutaminase (vertaling onbekend)blaD006655D08.586.277.087.520Histone DeacetylaseHistone Deacetylase (vertaling onbekend)Hydrolyzes N-acetyl groups on histones.D009535D08.586.277.087.610NicotinamidaseNicotinamidase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of nicotinamide to nicotinate and ammonia. EC 3.5.1.19.D010399D08.586.277.087.690Penicillin AmidasePenicillin Amidase (vertaling onbekend)An enzyme catalyzing the hydrolysis of penicillin to penicin and a carboxylic acid anion. EC 3.5.1.11.D011752D08.586.277.087.760Pyroglutamate HydrolasePyroglutamate Hydrolase (vertaling onbekend)Hydrolyzes pyroglutamic acid in the presence of ATP to glutamate plus ADP and inorganic phosphate. Deficiency leads to pyroglutamic acidurea.D014510D08.586.277.087.902UreaseUrease (vertaling onbekend)An enzyme that catalyzes the conversion of urea and water to carbon dioxide and ammonia. EC 3.5.1.5.D000619D08.586.277.151AminohydrolasesAminohydrolases (vertaling onbekend)blaD006136D08.586.277.151.300GTP CyclohydrolaseGTP Cyclohydrolase (vertaling onbekend)(GTP cyclohydrolase I) or GTP 7,8-8,9-dihydrolase (pyrophosphate-forming) (GTP cyclohydrolase II). An enzyme group that hydrolyzes the imidazole ring of GTP, releasing carbon-8 as formate. Two C-N bonds are hydrolyzed and the pentase unit is isomerized. TD006148D08.586.277.151.350Guanine DeaminaseGuanine Deaminase (vertaling onbekend)An enzyme that catalyzes the deamination of guanine to form xanthine. EC 3.5.4.3.D009700D08.586.277.151.486Nucleoside DeaminasesNucleoside Deaminases (vertaling onbekend)Catalyze the hydrolysis of nucleosides with the elimination of ammonia.D000243D08.586.277.151.486.075Adenosine DeaminaseAdenosine Deaminase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of adenosine to inosine with the elimination of ammonia. Since there are wide tissue and species variations in the enzyme, it has been used as a tool in the study of human and animal genetics and in medical diagnosiD003564D08.586.277.151.486.250Cytidine DeaminaseCytidine Deaminase (vertaling onbekend)An enzyme that catalyzes the deamination of cytidine, forming uridine. EC 3.5.4.5.D009709D08.586.277.151.653Nucleotide DeaminasesNucleotide Deaminases (vertaling onbekend)Catalyze the hydrolysis of nucleotides with the elimination of ammonia.D000659D08.586.277.151.653.060AMP DeaminaseAMP Deaminase (vertaling onbekend)An enzyme that catalyzes the deamination of AMP to IMP. EC 3.5.4.6.D003844D08.586.277.151.653.200DCMP DeaminaseDCMP Deaminase (vertaling onbekend)An enzyme that catalyzes the hydrolytic deamination of deoxycytidylic acid to deoxyuridylic acid and ammonia. It plays an important role in the regulation of the pool of deoxynucleotides in higher organisms. The enzyme also acts on some 5-substituted deoxD003166D08.586.277.300Complement Activating EnzymesComplement Activating Enzymes (vertaling onbekend)Enzymes present in the complement system which activate one or more components in the system.D015923D08.586.277.300.280Complement 1rComplement 1r (vertaling onbekend)Subcomponent of complement 1 which, when activated by C1q, activates subcomponent C1s by proteolytic cleavage.D003173D08.586.277.300.290Complement 1sComplement 1s (vertaling onbekend)The activated form of complement 1 which has hydrolase activity. In the classical pathway, it splits first C4 and then C2 into active components, thereby generating a new enzyme referred to as EAC142 or C42 or C3 convertase.D003177D08.586.277.300.325Complement 3 ConvertaseComplement 3 Convertase (vertaling onbekend)The enzyme which in both the classical and alternate complement pathways cleaves complement 3 into anaphylatoxin (C3a) and C3b.D011416D08.586.277.300.450Complement Factor DComplement Factor D (vertaling onbekend)A serum protein which during the alternate pathway of complement activation converts the inactive factor B to COMPLEMENT 3 CONVERTASE. EC 3.4.21.46.D004851D08.586.277.340Epoxide HydrolasesEpoxide Hydrolases (vertaling onbekend)Enzymes that catalyze reversibly the formation of an epoxide or arene oxide from a glycol or aromatic diol, respectively. EC 3.3.2.3.D004950D08.586.277.352EsterasesEsterases (vertaling onbekend)blaD002265D08.586.277.352.100Carboxylic Ester HydrolasesCarboxylic Ester Hydrolases (vertaling onbekend)Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.D000115D08.586.277.352.100.050AcetylesteraseAcetylesterase (vertaling onbekend)An enzyme that catalyzes the conversion of acetate esters and water to alcohols and acetate. EC 3.1.1.6.D002787D08.586.277.352.100.150Cholesterol EsteraseCholesterol Esterase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of cholesterol and some other sterol esters, to liberate cholesterol plus a fatty acid anion. EC 3.1.1.13.D002802D08.586.277.352.100.170CholinesterasesCholinesterases (vertaling onbekend)blaD000110D08.586.277.352.100.170.176AcetylcholinesteraseAcetylcholinesterase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of ACETYLCHOLINE to CHOLINE and ACETATE. In the CNS, this enzyme plays a role in the function of peripheral neuromuscular junctions. EC 3.1.1.7.D002091D08.586.277.352.100.170.250ButyrylcholinesteraseButyrylcholinesterase (vertaling onbekend)An aspect of cholinesterase (EC 3.1.1.8).D011543D08.586.277.352.100.170.710PseudocholinesterasePseudocholinesterase (vertaling onbekend)An aspect of cholinesterases.D003682D08.586.277.352.100.220DehydroascorbataseDehydroascorbatase (vertaling onbekend)Catalyzes the hydrolysis of the gamma lactone, dehydroascorbate, to diketogulonate.D008049D08.586.277.352.100.400LipaseLipase (vertaling onbekend)An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. It is produced by glands on the tongue and by the pancreas and initiates the digestion of dietary fats. (From DorlandD020799D08.586.277.352.100.400.745PancrelipasePancrelipase (vertaling onbekend)A preparation of hog pancreatic enzymes standardized for lipase content.D008071D08.586.277.352.100.430Lipoprotein LipaseLipoprotein Lipase (vertaling onbekend)An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. The enzyme hydrolyzes triacylglycerols in chylomicrons, very-low-density lipoproteins, low-density lipoproteins, and D008994D08.586.277.352.100.500Monoacylglycerol LipasesMonoacylglycerol Lipases (vertaling onbekend)An enzyme that catalyzes the hydrolysis of glycerol monoesters of long-chain fatty acids EC 3.1.1.23.D009283D08.586.277.352.100.550Naphthol AS D EsteraseNaphthol AS D Esterase (vertaling onbekend)Hydrolytic enzyme activity used as a histocytochemical test for the presence of esterases in tissue. Substrate used is 3-hydroxy-4'-nitro-2-naphthanilide chloroacetate (naphthol AS-D).D010740D08.586.277.352.100.680PhospholipasesPhospholipases (vertaling onbekend)A class of enzymes that catalyze the hydrolysis of phosphoglycerides or glycerophosphatidates. EC 3.1.-.D008245D08.586.277.352.100.680.510LysophospholipaseLysophospholipase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of a single fatty acid ester bond in lysoglycerophosphatidates with the formation of glyceryl phosphatidates and a fatty acid. EC 3.1.1.5.D010741D08.586.277.352.100.680.750Phospholipases APhospholipases A (vertaling onbekend)Phosphatide acylhydrolases. Catalyze the hydrolysis of one of the acyl groups of phosphoglycerides or glycerophosphatidates. Phospholipase A1 hydrolyzes the acyl group attached to the 1-position (EC 3.1.1.32) and phospholipase A2 hydrolyzes the acyl groupD003851D08.586.277.352.335DeoxyribonucleasesDeoxyribonucleases (vertaling onbekend)Enzymes which catalyze the hydrolases of ester bonds within DNA. EC 3.1.-.D004706D08.586.277.352.335.350EndodeoxyribonucleasesEndodeoxyribonucleases (vertaling onbekend)A group of enzymes catalyzing the endonucleolytic cleavage of DNA. They include members of EC 3.1.21.-, EC 3.1.22.-, EC 3.1.23.- (DNA RESTRICTION ENZYMES), EC 3.1.24.- (DNA RESTRICTION ENZYMES), and EC 3.1.25.-.D015719D08.586.277.352.335.350.025Aspergillus Nuclease S1Aspergillus Nuclease S1 (vertaling onbekend)An enzyme that catalyzes endonucleolytic cleavage to 5-phosphomononucleotides and 5-phosphooligonucleotide end-products. It has a preference for single-stranded substrates but is active with either ribo- or deoxyribonucleic acids. (From Enzyme NomenclaturD003850D08.586.277.352.335.350.250Deoxyribonuclease IDeoxyribonuclease I (vertaling onbekend)An enzyme capable of hydrolyzing highly polymerized DNA by splitting phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide. This catalyzes endonucleolytic cleavage of DNA yielding 5'-phosphodi- and oligonucleotide end-products. D013299D08.586.277.352.335.350.250.900Streptodornase and StreptokinaseStreptodornase and Streptokinase (vertaling onbekend)A mixture of the enzymes (streptokinase and streptodornase) produced by hemolytic streptococci. It is used topically on surface lesions and by instillation in closed body cavities to remove clotted blood or fibrinous or purulent accumulations. It is also D004262D08.586.277.352.335.350.300DNA Restriction EnzymesDNA Restriction Enzymes (vertaling onbekend)Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded D015253D08.586.277.352.335.350.300.250Deoxyribonucleases, Type I Site-SpecificDeoxyribonucleases, Type I Site-Specific (vertaling onbekend)Enzyme systems containing three different subunits and requiring ATP, S-adenosylmethionine, and magnesium for endonucleolytic activity to give random double-stranded fragments with terminal 5'-phosphates. They function also as DNA-dependent ATPases aD015252D08.586.277.352.335.350.300.260Deoxyribonucleases, Type II Site-SpecificDeoxyribonucleases, Type II Site-Specific (vertaling onbekend)Enzyme systems containing a single subunit and requiring only magnesium for endonucleolytic activity. The corresponding modification methylases are separate enzymes. The systems recognize specific short DNA sequences and cleave either within, or at a shorD015245D08.586.277.352.335.350.300.260.240Deoxyribonuclease BamHIDeoxyribonuclease BamHI (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence G/GATCC at the slash. BamHI is from Bacillus amyloliquefaciens N. Numerous isoschizomers have been identified. EC 3.1.21.-.D015246D08.586.277.352.335.350.300.260.250Deoxyribonuclease EcoRIDeoxyribonuclease EcoRI (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence G/AATTC at the slash. EcoRI is from E coliRY13. Several isoschizomers have been identified. EC 3.1.21.-.D015247D08.586.277.352.335.350.300.260.260Deoxyribonuclease HindIIIDeoxyribonuclease HindIII (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence A/AGCTT at the slash. HindIII is from Haemophilus influenzae R(d). Numerous isoschizomers have been identified. EC 3.1.21.-.D019003D08.586.277.352.335.350.300.260.300Deoxyribonuclease HpaIIDeoxyribonuclease HpaII (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequences C/CGG and GGC/C at the slash. HpaII is from Haemophilus parainfluenzae. Several isoschizomers have been identified. EC 3.1.21.-.D015263D08.586.277.352.335.350.300.270Deoxyribonucleases, Type III Site-SpecificDeoxyribonucleases, Type III Site-Specific (vertaling onbekend)Enzyme systems composed of two subunits and requiring ATP and magnesium for endonucleolytic activity; they do not function as ATPases. They exist as complexes with modification methylases of similar specificity listed under EC 2.1.1.72 or EC 2.1.1.73. TheD008836D08.586.277.352.335.350.500Micrococcal NucleaseMicrococcal Nuclease (vertaling onbekend)An enzyme that catalyzes the endonucleolytic cleavage to 3'-phosphomononucleotide and 3'-phospholigonucleotide end-products. It can cause hydrolysis of double- or single-stranded DNA or RNA. (From Enzyme Nomenclature, 1992) EC 3.1.31.1.D005090D08.586.277.352.335.375ExodeoxyribonucleasesExodeoxyribonucleases (vertaling onbekend)A family of enzymes that catalyze the exonucleolytic cleavage of DNA. It includes members of the class EC 3.1.11 that produce 5'-phosphomonoesters as cleavage products. EC 3.1.-.D004720D08.586.277.352.355EndonucleasesEndonucleases (vertaling onbekend)Enzymes that catalyze the hydrolysis of the internal bonds and thereby the formation of polynucleotides or oligonucleotides from ribo- or deoxyribonucleotide chains. EC 3.1.-.D004706D08.586.277.352.355.325EndodeoxyribonucleasesEndodeoxyribonucleases (vertaling onbekend)A group of enzymes catalyzing the endonucleolytic cleavage of DNA. They include members of EC 3.1.21.-, EC 3.1.22.-, EC 3.1.23.- (DNA RESTRICTION ENZYMES), EC 3.1.24.- (DNA RESTRICTION ENZYMES), and EC 3.1.25.-.D015719D08.586.277.352.355.325.025Aspergillus Nuclease S1Aspergillus Nuclease S1 (vertaling onbekend)An enzyme that catalyzes endonucleolytic cleavage to 5-phosphomononucleotides and 5-phosphooligonucleotide end-products. It has a preference for single-stranded substrates but is active with either ribo- or deoxyribonucleic acids. (From Enzyme NomenclaturD004262D08.586.277.352.355.325.300DNA Restriction EnzymesDNA Restriction Enzymes (vertaling onbekend)Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded D015253D08.586.277.352.355.325.300.250Deoxyribonucleases, Type I Site-SpecificDeoxyribonucleases, Type I Site-Specific (vertaling onbekend)Enzyme systems containing three different subunits and requiring ATP, S-adenosylmethionine, and magnesium for endonucleolytic activity to give random double-stranded fragments with terminal 5'-phosphates. They function also as DNA-dependent ATPases aD015252D08.586.277.352.355.325.300.260Deoxyribonucleases, Type II Site-SpecificDeoxyribonucleases, Type II Site-Specific (vertaling onbekend)Enzyme systems containing a single subunit and requiring only magnesium for endonucleolytic activity. The corresponding modification methylases are separate enzymes. The systems recognize specific short DNA sequences and cleave either within, or at a shorD015245D08.586.277.352.355.325.300.260.240Deoxyribonuclease BamHIDeoxyribonuclease BamHI (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence G/GATCC at the slash. BamHI is from Bacillus amyloliquefaciens N. Numerous isoschizomers have been identified. EC 3.1.21.-.D015246D08.586.277.352.355.325.300.260.250Deoxyribonuclease EcoRIDeoxyribonuclease EcoRI (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence G/AATTC at the slash. EcoRI is from E coliRY13. Several isoschizomers have been identified. EC 3.1.21.-.D015247D08.586.277.352.355.325.300.260.260Deoxyribonuclease HindIIIDeoxyribonuclease HindIII (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence A/AGCTT at the slash. HindIII is from Haemophilus influenzae R(d). Numerous isoschizomers have been identified. EC 3.1.21.-.D019003D08.586.277.352.355.325.300.260.300Deoxyribonuclease HpaIIDeoxyribonuclease HpaII (vertaling onbekend)One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequences C/CGG and GGC/C at the slash. HpaII is from Haemophilus parainfluenzae. Several isoschizomers have been identified. EC 3.1.21.-.D015263D08.586.277.352.355.325.300.270Deoxyribonucleases, Type III Site-SpecificDeoxyribonucleases, Type III Site-Specific (vertaling onbekend)Enzyme systems composed of two subunits and requiring ATP and magnesium for endonucleolytic activity; they do not function as ATPases. They exist as complexes with modification methylases of similar specificity listed under EC 2.1.1.72 or EC 2.1.1.73. TheD008836D08.586.277.352.355.325.500Micrococcal NucleaseMicrococcal Nuclease (vertaling onbekend)An enzyme that catalyzes the endonucleolytic cleavage to 3'-phosphomononucleotide and 3'-phospholigonucleotide end-products. It can cause hydrolysis of double- or single-stranded DNA or RNA. (From Enzyme Nomenclature, 1992) EC 3.1.31.1.D004722D08.586.277.352.355.350EndoribonucleasesEndoribonucleases (vertaling onbekend)A family of enzymes that catalyze the endonucleolytic cleavage of RNA. It includes EC 3.1.26.-, EC 3.1.27.-, EC 3.1.30.-, and EC 3.1.31.-.D015719D08.586.277.352.355.350.025Aspergillus Nuclease S1Aspergillus Nuclease S1 (vertaling onbekend)An enzyme that catalyzes endonucleolytic cleavage to 5-phosphomononucleotides and 5-phosphooligonucleotide end-products. It has a preference for single-stranded substrates but is active with either ribo- or deoxyribonucleic acids. (From Enzyme NomenclaturD008836D08.586.277.352.355.350.500Micrococcal NucleaseMicrococcal Nuclease (vertaling onbekend)An enzyme that catalyzes the endonucleolytic cleavage to 3'-phosphomononucleotide and 3'-phospholigonucleotide end-products. It can cause hydrolysis of double- or single-stranded DNA or RNA. (From Enzyme Nomenclature, 1992) EC 3.1.31.1.D016914D08.586.277.352.355.350.700Ribonuclease H, Calf ThymusRibonuclease H, Calf Thymus (vertaling onbekend)A ribonuclease that specifically cleaves the RNA moiety of RNA:DNA hybrids. It has been isolated from a wide variety of prokaryotic and eukaryotic organisms (particularly calf thymus) as well as retroviruses. EC 3.1.26.4.D012259D08.586.277.352.355.350.715Ribonuclease, PancreaticRibonuclease, Pancreatic (vertaling onbekend)An enzyme that catalyzes the endonucleolytic cleavage of pancreatic ribonucleic acids to 3'-phosphomono- and oligonucleotides ending in cytidylic or uridylic acids with 2',3'-cyclic phosphate intermediates. EC 3.1.27.5.D006163D08.586.277.352.355.350.725Ribonuclease T1Ribonuclease T1 (vertaling onbekend)An enzyme catalyzing the endonucleolytic cleavage of RNA at the 3'-position of a guanylate residue. EC 3.1.27.3.D005092D08.586.277.352.365ExonucleasesExonucleases (vertaling onbekend)Enzymes that catalyze the release of mononucleotides by the hydrolysis of the terminal bond of deoxyribonucleotide or ribonucleotide chains. EC 3.1.-.D005090D08.586.277.352.365.290ExodeoxyribonucleasesExodeoxyribonucleases (vertaling onbekend)A family of enzymes that catalyze the exonucleolytic cleavage of DNA. It includes members of the class EC 3.1.11 that produce 5'-phosphomonoesters as cleavage products. EC 3.1.-.D005095D08.586.277.352.365.300ExoribonucleasesExoribonucleases (vertaling onbekend)A family of enzymes that catalyze the exonucleolytic cleavage of RNA. It includes EC 3.1.13.-, EC 3.1.14.-, EC 3.1.15.-, and EC 3.1.16.-. EC 3.1.-D010727D08.586.277.352.640Phosphoric Diester HydrolasesPhosphoric Diester Hydrolases (vertaling onbekend)A class of enzymes that catalyze the hydrolysis of one of the two ester bonds in a phosphodiester compound. EC 3.1.4.D017318D08.586.277.352.640.050Annexin IIIAnnexin III (vertaling onbekend)A protein of the annexin family that catalyzes the conversion of 1-D-inositol 1,2-cyclic phosphate and water to 1-D-myo-inositol 1-phosphate. EC 3.1.4.36.D015106D08.586.277.352.640.1253',5'-Cyclic-GMP Phosphodiesterase3',5'-Cyclic-GMP Phosphodiesterase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of cyclic GMP to yield guanosine-5'-phosphate. EC 3.1.4.35.D015105D08.586.277.352.640.1503',5'-Cyclic-Nucleotide Phosphodiesterase3',5'-Cyclic-Nucleotide Phosphodiesterase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of cyclic AMP to form adenosine 5'-phosphate. The enzyme is widely distributed in animal tissue and controls the level of intracellular cyclic AMP. Also acts on 3',5'-cyclic IMP and 3',5'-cyD015087D08.586.277.352.640.1602',3'-Cyclic-Nucleotide Phosphodiesterases2',3'-Cyclic-Nucleotide Phosphodiesterases (vertaling onbekend)Nucleoside-2',3'-cyclic phosphate nucleotidohydrolase. Enzymes that catalyze the hydrolysis of the 2'- or 3'- phosphate bonds of 2',3'-cyclic nucleotides. Also hydrolyzes nucleoside monophosphates. Includes EC 3.1.4.16 and ECD010740D08.586.277.352.640.700PhospholipasesPhospholipases (vertaling onbekend)A class of enzymes that catalyze the hydrolysis of phosphoglycerides or glycerophosphatidates. EC 3.1.-.D010738D08.586.277.352.640.700.700Phospholipase CPhospholipase C (vertaling onbekend)An enzyme found in the alpha-toxin of Clostridium welchii and other strains of clostridia and bacilli. It hydrolyzes glycerophosphatidates with the formation of 1,2-diacylglycerol and a phosphorylated nitrogenous base such as choline. EC 3.1.4.3.D010739D08.586.277.352.640.700.710Phospholipase DPhospholipase D (vertaling onbekend)An enzyme found mostly in plant tissue. It hydrolyzes glycerophosphatidates with the formation of a phosphatidic acid and a nitrogenous base such as choline. This enzyme also catalyzes transphosphatidylation reactions. EC 3.1.4.4.D013108D08.586.277.352.640.750Sphingomyelin PhosphodiesteraseSphingomyelin Phosphodiesterase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of sphingomyelin to ceramide (N-acylsphingosine) plus choline phosphate. A defect in this enzyme leads to NIEMANN-PICK DISEASE. EC 3.1.4.12.D010744D08.586.277.352.650Phosphoric Monoester HydrolasesPhosphoric Monoester Hydrolases (vertaling onbekend)A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.D000135D08.586.277.352.650.025Acid PhosphataseAcid Phosphatase (vertaling onbekend)An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.D000469D08.586.277.352.650.035Alkaline PhosphataseAlkaline Phosphatase (vertaling onbekend)An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.D006597D08.586.277.352.650.200Fructose-BisphosphataseFructose-Bisphosphatase (vertaling onbekend)An enzyme that catalyzes the conversion of D-fructose 1,6-bisphosphate and water to D-fructose 6-phosphate and orthophosphate. EC 3.1.3.11.D005952D08.586.277.352.650.225Glucose-6-PhosphataseGlucose-6-Phosphatase (vertaling onbekend)An enzyme that catalyzes the conversion of D-glucose 6-phosphate and water to D-glucose and orthophosphate. EC 3.1.3.9.D006642D08.586.277.352.650.300Histidinol-PhosphataseHistidinol-Phosphatase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of histidinol-phosphate to histidinol. One of the regulatory enzymes in histidine biosynthesis. EC 3.1.3.15.D009597D08.586.277.352.650.5754-Nitrophenylphosphatase4-Nitrophenylphosphatase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of nitrophenyl phosphates to nitrophenols. At acid pH it is probably ACID PHOSPHATASE (EC 3.1.3.2); at alkaline pH it is probably ALKALINE PHOSPHATASE (EC 3.1.3.1). EC 3.1.3.41.D009708D08.586.277.352.650.600NucleotidasesNucleotidases (vertaling onbekend)A class of enzymes that catalyze the conversion of a nucleotide and water to a nucleoside and orthophosphate. EC 3.1.3.-.D015720D08.586.277.352.650.600.6005'-Nucleotidase5'-Nucleotidase (vertaling onbekend)A glycoprotein enzyme present in various organs and in many cells. The enzyme catalyzes the hydrolysis of a 5'-ribonucleotide to a ribonucleoside and orthophosphate in the presence of water. It is cation-dependent and exists in a membrane-bound and sD010711D08.586.277.352.650.620Phosphatidate PhosphatasePhosphatidate Phosphatase (vertaling onbekend)A phosphomonoesterase involved in the synthesis of triacylglycerols. It catalyzes the hydrolysis of phosphatidates with the formation of diacylglycerols and orthophosphate. EC 3.1.3.4.D025481D08.586.277.352.650.622Phosphofructokinase-2Phosphofructokinase-2 (vertaling onbekend)An allosteric enzyme that regulates glycolysis and gluconeogenesis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-2,6-bisphosphate, an allosteric effector for the other 6-phosphofructokinase, PHOSPHOFRUCD010749D08.586.277.352.650.625Phosphoprotein PhosphatasePhosphoprotein Phosphatase (vertaling onbekend)A group of enzymes removing the serine- or threonine-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992) EC 3.1.3.16.D019703D08.586.277.352.650.625.150CalcineurinCalcineurin (vertaling onbekend)A calcium- and calmodulin-binding protein present in highest concentrations in the central nervous system. Calcineurin is composed of two subunits. A catalytic subunit, calcineurin A, and a regulatory subunit, calcineurin B, with molecular weights of abouD006007D08.586.277.352.650.625.300Glycogen-Synthase-D PhosphataseGlycogen-Synthase-D Phosphatase (vertaling onbekend)An enzyme that catalyzes the conversion of phosphorylated, inactive glycogen synthase D to active dephosphoglycogen synthase I. EC 3.1.3.42.D010765D08.586.277.352.650.625.650Phosphorylase PhosphatasePhosphorylase Phosphatase (vertaling onbekend)An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. EC 3.1.3.17.D017027D08.586.277.352.650.625.700Protein-Tyrosine-PhosphataseProtein-Tyrosine-Phosphatase (vertaling onbekend)An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cellD017493D08.586.277.352.650.625.700.150Antigens, CD45Antigens, CD45 (vertaling onbekend)High-molecular weight glycoproteins uniquely expressed on the surface of all leukocytes and their hemopoietic progenitors. The CD45 family consists of multiple members that are all products of a single gene. CD45 expression is necessary for signalling thrD020687D08.586.277.352.650.625.700.200cdc25 Phosphatasecdc25 Phosphatase (vertaling onbekend)A tyrosine phosphatase required for progression of the cell cycle. It is required for p34(cdc2) kinase activation.D011769D08.586.277.352.650.625.725Pyruvate Dehydrogenase (Lipoamide)-PhosphatasePyruvate Dehydrogenase (Lipoamide)-Phosphatase (vertaling onbekend)(Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43.D010832D08.586.277.352.650.7006-Phytase6-Phytase (vertaling onbekend)An enzyme that catalyzes the conversion of myo-inositol hexakisphosphate and water to 1L-myo-inositol 1,2,3,4,5-pentakisphosphate and orthophosphate. EC 3.1.3.26.D012260D08.586.277.352.700RibonucleasesRibonucleases (vertaling onbekend)Enzymes that catalyze the hydrolysis of ester bonds within RNA. EC 3.1.-.D004722D08.586.277.352.700.350EndoribonucleasesEndoribonucleases (vertaling onbekend)A family of enzymes that catalyze the endonucleolytic cleavage of RNA. It includes EC 3.1.26.-, EC 3.1.27.-, EC 3.1.30.-, and EC 3.1.31.-.D015719D08.586.277.352.700.350.025Aspergillus Nuclease S1Aspergillus Nuclease S1 (vertaling onbekend)An enzyme that catalyzes endonucleolytic cleavage to 5-phosphomononucleotides and 5-phosphooligonucleotide end-products. It has a preference for single-stranded substrates but is active with either ribo- or deoxyribonucleic acids. (From Enzyme NomenclaturD008836D08.586.277.352.700.350.500Micrococcal NucleaseMicrococcal Nuclease (vertaling onbekend)An enzyme that catalyzes the endonucleolytic cleavage to 3'-phosphomononucleotide and 3'-phospholigonucleotide end-products. It can cause hydrolysis of double- or single-stranded DNA or RNA. (From Enzyme Nomenclature, 1992) EC 3.1.31.1.D016914D08.586.277.352.700.350.700Ribonuclease H, Calf ThymusRibonuclease H, Calf Thymus (vertaling onbekend)A ribonuclease that specifically cleaves the RNA moiety of RNA:DNA hybrids. It has been isolated from a wide variety of prokaryotic and eukaryotic organisms (particularly calf thymus) as well as retroviruses. EC 3.1.26.4.D012259D08.586.277.352.700.350.715Ribonuclease, PancreaticRibonuclease, Pancreatic (vertaling onbekend)An enzyme that catalyzes the endonucleolytic cleavage of pancreatic ribonucleic acids to 3'-phosphomono- and oligonucleotides ending in cytidylic or uridylic acids with 2',3'-cyclic phosphate intermediates. EC 3.1.27.5.D006163D08.586.277.352.700.350.725Ribonuclease T1Ribonuclease T1 (vertaling onbekend)An enzyme catalyzing the endonucleolytic cleavage of RNA at the 3'-position of a guanylate residue. EC 3.1.27.3.D005095D08.586.277.352.700.375ExoribonucleasesExoribonucleases (vertaling onbekend)A family of enzymes that catalyze the exonucleolytic cleavage of RNA. It includes EC 3.1.13.-, EC 3.1.14.-, EC 3.1.15.-, and EC 3.1.16.-. EC 3.1.-D013429D08.586.277.352.827SulfatasesSulfatases (vertaling onbekend)blaD001192D08.586.277.352.827.070ArylsulfatasesArylsulfatases (vertaling onbekend)Enzymes that catalyze the hydrolysis of a phenol sulfate to yield a phenol and sulfate. Arylsulfatase A, B, and C have been separated. A deficiency of arylsulfatases is one of the causes of metachromatic leukodystrophy (LEUKODYSTROPHY, METACHROMATIC). EC D020051D08.586.277.352.827.070.060N-Acetylgalactosamine-4-SulfataseN-Acetylgalactosamine-4-Sulfatase (vertaling onbekend)An arylsulfatase that catalyzes the hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate. A deficiency of this enzyme is responsible for the inherited lysosomal disease, Maroteaux-LD002553D08.586.277.352.827.070.250Cerebroside-SulfataseCerebroside-Sulfatase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of cerebroside 3-sulfate (sulfatide) to yield a cerebroside and inorganic sulfate. A marked deficiency of arylsulfatase A, which is considered the heat-labile component of cerebroside sulfatase, has been demonstrateD002810D08.586.277.352.827.180Chondroitinases and Chondroitin LyasesChondroitinases and Chondroitin Lyases (vertaling onbekend)Enzymes which catalyze the elimination of glucuronate residues from chondroitin A,B, and C or which catalyze the hydrolysis of sulfate groups of the 2-acetamido-2-deoxy-D-galactose 6-sulfate units of chondroitin sulfate. EC 4.2.2.-.D002811D08.586.277.352.827.180.175ChondroitinsulfatasesChondroitinsulfatases (vertaling onbekend)A group of enzymes that catalyze the hydrolysis of various sulfate bonds of chondroitin sulfate. EC 3.1.6.-.D020051D08.586.277.352.827.180.175.060N-Acetylgalactosamine-4-SulfataseN-Acetylgalactosamine-4-Sulfatase (vertaling onbekend)An arylsulfatase that catalyzes the hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate. A deficiency of this enzyme is responsible for the inherited lysosomal disease, Maroteaux-LD002803D08.586.277.352.827.180.175.275Chondro-4-SulfataseChondro-4-Sulfatase (vertaling onbekend)An enzyme from the sulfuric ester hydrolase class that breaks down one of the products of the chondroitin lyase II reaction. EC 3.1.6.9.D007066D08.586.277.352.827.500Iduronate SulfataseIduronate Sulfatase (vertaling onbekend)An enzyme that specifically cleaves the ester sulfate of iduronic acid. Its deficiency has been demonstrated in Hunter's syndrome, which is characterized by an excess of dermatan sulfate and heparan sulfate. EC 3.1.6.13.D013869D08.586.277.352.897Thiolester HydrolasesThiolester Hydrolases (vertaling onbekend)blaD000104D08.586.277.352.897.075Acetyl-CoA HydrolaseAcetyl-CoA Hydrolase (vertaling onbekend)An enzyme that catalyzes reversibly the hydrolysis of acetyl-CoA to yield CoA and acetate. The enzyme is involved in the oxidation of fatty acids. EC 3.1.2.1.D010170D08.586.277.352.897.700Palmitoyl-CoA HydrolasePalmitoyl-CoA Hydrolase (vertaling onbekend)Enzyme catalyzing reversibly the hydrolysis of palmitoyl-CoA or other long-chain acyl coenzyme A compounds to yield CoA and palmitate or other acyl esters. The enzyme is involved in the esterification of fatty acids to form triglycerides. EC 3.1.2.2.D006026D08.586.277.450Glycoside HydrolasesGlycoside Hydrolases (vertaling onbekend)blaD000681D08.586.277.450.066AmylasesAmylases (vertaling onbekend)A group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-.D000516D08.586.277.450.066.050alpha-Amylasealpha-Amylase (vertaling onbekend)An enzyme that catalyzes the endohydrolysis of 1,4-alpha-glycosidic linkages in starch, glycogen, and related polysaccharides and oligosaccharides containing 3 or more 1,4-alpha-linked D-glucose units. EC 3.2.1.1.D001614D08.586.277.450.066.100beta-Amylasebeta-Amylase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of 1,4-alpha-glycosidic linkages in starch, glycogen, and related polysaccharides and oligosaccharides so as to remove successive beta-maltose units from the non-reducing ends of the chains. EC 3.2.1.2.D002480D08.586.277.450.162CellulaseCellulase (vertaling onbekend)An enzyme isolated from fungi and bacteria. It catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin, and cereal beta-glucans. EC 3.2.1.4.D002688D08.586.277.450.207ChitinaseChitinase (vertaling onbekend)blaD003910D08.586.277.450.283DextranaseDextranase (vertaling onbekend)blaD004186D08.586.277.450.329DisaccharidasesDisaccharidases (vertaling onbekend)blaD013393D08.586.277.450.329.738SucraseSucrase (vertaling onbekend)blaD013394D08.586.277.450.329.738.700Sucrase-Isomaltase ComplexSucrase-Isomaltase Complex (vertaling onbekend)An enzyme complex found in the brush border membranes of the small intestine. It is believed to be an enzyme complex with different catalytic sites. Its absence is manifested by an inherited disease called sucrase-isomaltase deficiency.D014198D08.586.277.450.329.865TrehalaseTrehalase (vertaling onbekend)An enzyme that catalyzes the conversion of alpha,alpha-trehalose and water to D-glucose. EC 3.2.1.28.D005644D08.586.277.450.400alpha-L-Fucosidasealpha-L-Fucosidase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of an alpha L-fucoside to yield an alcohol and L-fucose. Deficiency of this enzyme can cause FUCOSIDOSIS. EC 3.2.1.51.D005696D08.586.277.450.410GalactosidasesGalactosidases (vertaling onbekend)A family of galactoside hydrolases that hydrolyze compounds with an O-galactosyl linkage. EC 3.2.1.-.D000519D08.586.277.450.410.050alpha-Galactosidasealpha-Galactosidase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-galactosides including galactose oligosaccharides, galactomannans, and galactolipids. EC 3.2.1.22.D001616D08.586.277.450.410.100beta-Galactosidasebeta-Galactosidase (vertaling onbekend)A group of enzymes that catalyzes the hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-galactosides. Deficiency of beta-Galactosidase A1 may cause GANGLIOSIDOSIS GM1.D002517D08.586.277.450.410.150Ceramide TrihexosidaseCeramide Trihexosidase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of a ceramidetrihexoside to a ceramidedihexoside plus galactose. EC 3.2.1.47.D005698D08.586.277.450.410.400GalactosylceramidaseGalactosylceramidase (vertaling onbekend)An enzyme that hydrolyzes galactose from ceramide monohexosides. Deficiency of this enzyme may cause globoid cell leukodystrophy (LEUKODYSTROPHY, GLOBOID CELL). EC 3.2.1.46.D004693D08.586.277.450.415Glucan Endo-1,3-beta-D-GlucosidaseGlucan Endo-1,3-beta-D-Glucosidase (vertaling onbekend)An enzyme that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans including laminarin, paramylon, and pachyman. EC 3.2.1.39.D005959D08.586.277.450.420GlucosidasesGlucosidases (vertaling onbekend)Enzymes that hydrolyze O-glucosyl-compounds. (Enzyme Nomenclature, 1992) EC 3.2.1.-.D000520D08.586.277.450.420.050alpha-Glucosidasesalpha-Glucosidases (vertaling onbekend)Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II. EC 3.2.1.20.D001617D08.586.277.450.420.100beta-Glucosidasebeta-Glucosidase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of terminal non-reducing residues in beta-D-glucosides with release of beta-glucose. EC 3.2.1.21.D005087D08.586.277.450.420.375Glucan 1,4-alpha-GlucosidaseGlucan 1,4-alpha-Glucosidase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of polysaccharide chains with the release of beta-glucose. It is also able to hydrolyze 1,6-alpha-glucosidic bonds when the next boD006004D08.586.277.450.420.450Glycogen Debranching Enzyme SystemGlycogen Debranching Enzyme System (vertaling onbekend)1,4-alpha-D-Glucan-1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase/dextrin 6 alpha-D-glucanohydrolase. An enzyme system having both 4-alpha-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33) activities. As a transferase it transfersD010694D08.586.277.450.420.475GlycosylceramidaseGlycosylceramidase (vertaling onbekend)The enzyme hydrolyzing glycosyl-N-acylsphingosine to a sugar and N-acylsphingosine. It also catalyzes the hydrolysis of phlorizin to phloretin and glucose. It is found in the intestinal brush border membrane often in conjunction with lactase. EC 3.2.1.62.D005962D08.586.277.450.420.475.400GlucosylceramidaseGlucosylceramidase (vertaling onbekend)A glycosidase that hydrolyzes a glucosylceramide to yield free ceramide plus glucose. Deficiency of this enzyme leads to abnormally high concentrations of glucosylceramide in the brain in GAUCHER DISEASE. EC 3.2.1.45.D005966D08.586.277.450.426GlucuronidaseGlucuronidase (vertaling onbekend)blaD006596D08.586.277.450.483HexosaminidasesHexosaminidases (vertaling onbekend)Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on glucosides, galactosides, and several oligosaccharides.D001619D08.586.277.450.483.180beta-N-Acetylhexosaminidasebeta-N-Acetylhexosaminidase (vertaling onbekend)An enzyme hydrolyzing terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. It acts on glucosides, galactosides, and several oligosaccharides. Hexosaminidase A cleaves GM2, GA2, globosides, and hexosamine oligosaccharides.D005689D08.586.277.450.483.356GalactosaminidaseGalactosaminidase (vertaling onbekend)blaD005946D08.586.277.450.483.531GlucosaminidaseGlucosaminidase (vertaling onbekend)blaD000118D08.586.277.450.483.531.080AcetylglucosaminidaseAcetylglucosaminidase (vertaling onbekend)2-Acetamido-2-deoxy-beta-D-glucoside acetamidodeoxygluco-hydrolase. Catalyzes the hydrolysis of terminal, non-reducing 2-acetamido-2-deoxy-beta-glucose residues in chitobiose and higher analogs as well as in glycoproteins. Has been used widely in structurD017038D08.586.277.450.483.531.080.500Mannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase (vertaling onbekend)A group of related enzymes responsible for the endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose-content glycopeptides and glycoproteins. EC 3.2.1.96.D006821D08.586.277.450.529HyaluronoglucosaminidaseHyaluronoglucosaminidase (vertaling onbekend)An enzyme that catalyzes the random hydrolysis of 1,4-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate. (From Enzyme Nomenclature, 1992)D007068D08.586.277.450.560IduronidaseIduronidase (vertaling onbekend)An enzyme that hydrolyzes iduronosidic linkages in desulfated dermatan. Deficiency of this enzyme produces Hurler's syndrome. EC 3.2.1.76.D007517D08.586.277.450.585IsoamylaseIsoamylase (vertaling onbekend)An enzyme that hydrolyzes 1,6-alpha-glucosidic branch linkages in glycogen, amylopectin, and their beta-limit dextrins. It is distinguished from pullulanase (EC 3.2.1.41) by its inability to attack pullulan and by the feeble action of alpha-limit dextrinsD008361D08.586.277.450.625MannosidasesMannosidases (vertaling onbekend)alpha or beta-Mannoside mannohydrolases. Catalyzes the hydrolysis of terminal, non-reducing alpha or beta-D-mannose residues in mannosides. Deficiency of the alpha form can cause mannosidosis.D009113D08.586.277.450.642MuramidaseMuramidase (vertaling onbekend)A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidD009439D08.586.277.450.692NeuraminidaseNeuraminidase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. D009699D08.586.277.450.737NucleosidasesNucleosidases (vertaling onbekend)blaD009244D08.586.277.450.737.400NAD+ NucleosidaseNAD+ Nucleosidase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of NAD to nicotinamide and ADPribose. EC 3.2.2.5.D009834D08.586.277.450.770Oligo-1,6-GlucosidaseOligo-1,6-Glucosidase (vertaling onbekend)An enzyme that catalyzes the endohydrolysis of 1,6-alpha-glucosidic linkages in isomaltose and dextrins produced from starch and glycogen by alpha-amylase. EC 3.2.1.10.D013394D08.586.277.450.770.800Sucrase-Isomaltase ComplexSucrase-Isomaltase Complex (vertaling onbekend)An enzyme complex found in the brush border membranes of the small intestine. It is believed to be an enzyme complex with different catalytic sites. Its absence is manifested by an inherited disease called sucrase-isomaltase deficiency.D011096D08.586.277.450.800PolygalacturonasePolygalacturonase (vertaling onbekend)A cell wall-degrading enzyme found in microorganisms and higher plants. It catalyzes the random hydrolysis of 1,4-alpha-D-galactosiduronic linkages in pectate and other galacturonans. EC 3.2.1.15.D014995D08.586.277.450.950XylosidasesXylosidases (vertaling onbekend)A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages. EC 3.2.1.8 catalyzes the endo-hydrolysis of 1,4-beta-D-xylosidic linkages; EC 3.2.1.32 catalyzes the endo-hydrolysis of 1,3-beta-D-xylosidic linkages; EC 3.2.1.37 catalyD010194D08.586.277.610PancreatinPancreatin (vertaling onbekend)A mammalian pancreatic extract composed of enzymes with protease, amylase and lipase activities. It is used as a digestant in pancreatic malfunction.D010447D08.586.277.656Peptide HydrolasesPeptide Hydrolases (vertaling onbekend)A subclass of enzymes from the hydrolase class that catalyze the hydrolysis of peptide bonds. EXOPEPTIDASES and ENDOPEPTIDASES make up the sub-subclasses for this group. EC 3.4.D010450D08.586.277.656.300EndopeptidasesEndopeptidases (vertaling onbekend)A subclass of PEPTIDE HYDROLASES. They are classified primarily by their catalytic mechanism. Specificity is used only for identification of individual enzymes. They comprise the SERINE ENDOPEPTIDASES, EC 3.4.21; CYSTEINE ENDOPEPTIDASES, EC 3.4.22; ASPARTD016282D08.586.277.656.300.066Aspartic EndopeptidasesAspartic Endopeptidases (vertaling onbekend)A sub-subclass of ENDOPEPTIDASES that depend on an ASPARTIC ACID residue for their activity. EC 3.4.23.D002402D08.586.277.656.300.066.180Cathepsin DCathepsin D (vertaling onbekend)An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).D020059D08.586.277.656.300.066.185Cathepsin ECathepsin E (vertaling onbekend)An aspartic endopeptidase of the hydrolase class that is similar to cathepsin D but has a slightly broader specificity. EC 3.4.23.34.D012085D08.586.277.656.300.066.200ChymosinChymosin (vertaling onbekend)The predominant milk-clotting enzyme from the true stomach or abomasum of the suckling calf. It is secreted as an inactive precursor called prorennin and converted in the acid environment of the stomach to the active enzyme. EC 3.4.23.4.D016333D08.586.277.656.300.066.340HIV ProteaseHIV Protease (vertaling onbekend)Enzyme of the human immunodeficiency virus that is required for post-translational cleavage of gag and gag-pol precursor polyproteins into functional products needed for viral assembly. HIV protease is an aspartic protease encoded by the amino terminus ofD010434D08.586.277.656.300.066.700Pepsin APepsin A (vertaling onbekend)Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts asD012083D08.586.277.656.300.066.780ReninRenin (vertaling onbekend)An enzyme which is secreted by the kidney and is formed from prorenin in plasma and kidney. The enzyme cleaves the Leu-Leu bond in angiotensinogen to generate angiotensin I. EC 3.4.23.15. (Formerly EC 3.4.99.19).D001954D08.586.277.656.300.099BrinolaseBrinolase (vertaling onbekend)A fibrinolytic and thrombolytic enzyme from Aspergillus oryzae. EC 3.4.99.-.D002403D08.586.277.656.300.133CathepsinsCathepsins (vertaling onbekend)A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissue. They function optimally within an acidic pH range.D002401D08.586.277.656.300.133.125Cathepsin BCathepsin B (vertaling onbekend)A lysosomal cysteine proteinase which hydrolyzes proteins, with a specificity resembling that of papain. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been foD002402D08.586.277.656.300.133.187Cathepsin DCathepsin D (vertaling onbekend)An intracellular proteinase found in a variety of tissue. It has specificity similar to but narrower than that of pepsin A. The enzyme is involved in catabolism of cartilage and connective tissue. EC 3.4.23.5. (Formerly EC 3.4.4.23).D020059D08.586.277.656.300.133.250Cathepsin ECathepsin E (vertaling onbekend)An aspartic endopeptidase of the hydrolase class that is similar to cathepsin D but has a slightly broader specificity. EC 3.4.23.34.D020789D08.586.277.656.300.133.375Dipeptidyl Peptidase IDipeptidyl Peptidase I (vertaling onbekend)A cysteine-type peptidase that is CHLORINE dependent and functions maximally at acidic pHs. At neutral pH, it polymerizes esters, aryl- and dipeptide amides. EC 3.4.14.1.D003546D08.586.277.656.300.215Cysteine EndopeptidasesCysteine Endopeptidases (vertaling onbekend)ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by sulfhydryl reagents. EC 3.4.22.D001963D08.586.277.656.300.215.096BromelainsBromelains (vertaling onbekend)Protein-digesting and milk-clotting enzymes found in pineapple fruit juice and stem tissue. Enzymes from the two sources are distinguished as fruit bromelain and stem bromelain. They have anti-inflammatory activity and the enzymatic activity does not disaD002154D08.586.277.656.300.215.120CalpainCalpain (vertaling onbekend)Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including neuropeptides, cytoskeletal proteins, proteins from smooth muscle, cardiac muscle, liver, platelets and erythrocytes. Two subclasses having high and low calciD020169D08.586.277.656.300.215.126CaspasesCaspases (vertaling onbekend)A family of intracellular CYSTEINE ENDOPEPTIDASES. They play a key role in inflammation and mammalian APOPTOSIS. They are specific for aspartic acid at the P1 position. They are divided into two classes based on the lengths of their N-terminal prodomains.D020170D08.586.277.656.300.215.126.200Caspase 1Caspase 1 (vertaling onbekend)A member of the caspase family that is highly specific for interleukin-1beta (INTERLEUKIN-1). It plays a role in inflammation and mammalian APOPTOSIS. Interleukin-1beta converting enzyme is frequently abbreviated ICE. EC 3.4.22.36D002401D08.586.277.656.300.215.133Cathepsin BCathepsin B (vertaling onbekend)A lysosomal cysteine proteinase which hydrolyzes proteins, with a specificity resembling that of papain. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been foD002917D08.586.277.656.300.215.160ChymopapainChymopapain (vertaling onbekend)A cysteine endopeptidase isolated from papaya latex. Preferential cleavage at glutamic and aspartic acid residues. EC 3.4.22.6.D005361D08.586.277.656.300.215.350FicainFicain (vertaling onbekend)A sulfhydryl proteinase with cysteine at the active site from ficus latex. Preferential cleavage is at tyrosine and phenylalanine residues. EC 3.4.22.3.D010206D08.586.277.656.300.215.585PapainPapain (vertaling onbekend)A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.D008666D08.586.277.656.300.480MetalloendopeptidasesMetalloendopeptidases (vertaling onbekend)ENDOPEPTIDASES which use a metal, normally zinc, in the catalytic mechanism. This group of enzymes is inactivated by metal chelators. EC 3.4.24.D017364D08.586.277.656.300.480.205CollagenasesCollagenases (vertaling onbekend)Enzymes that catalyze the degradation of collagen by acting on the peptide bonds. EC 3.4.24.-.D020778D08.586.277.656.300.480.205.352Gelatinase AGelatinase A (vertaling onbekend)A secreted endopeptidase homologous with INTERSTITIAL COLLAGENASE, but which possesses an additional fibronectin-like domain. EC 3.4.24.24.D020780D08.586.277.656.300.480.205.360Gelatinase BGelatinase B (vertaling onbekend)An endopeptidase that is structurally similar to GELATINASE A. It degrades types I and V GELATIN and types IV and V COLLAGEN. EC 3.4.24.35.D020781D08.586.277.656.300.480.205.410Interstitial CollagenaseInterstitial Collagenase (vertaling onbekend)A member of the metalloproteinase family of enzymes that is principally responsible for cleaving fibrillar collagen. It can degrade interstitial collagens, types I, II and III. EC 3.4.24.7.D003012D08.586.277.656.300.480.205.500Microbial CollagenaseMicrobial Collagenase (vertaling onbekend)A metalloproteinase which degrades helical regions of native collagen to small fragments. Preferred cleavage is -Gly in the sequence -Pro-Xaa-Gly-Pro-. Six forms (or 2 classes) have been isolated from Clostridium histolyticum that are immunologically crosD020784D08.586.277.656.300.480.205.615Neutrophil CollagenaseNeutrophil Collagenase (vertaling onbekend)A member of the MATRIX METALLOPROTEINASES that cleaves triple-helical collagens types I, II, and III. EC 3.4.24.34.D018093D08.586.277.656.300.480.252GelatinasesGelatinases (vertaling onbekend)A class of enzymes that catalyzes the degradation of gelatin by acting on the peptide bonds. EC 3.4.24.-.D020778D08.586.277.656.300.480.252.420Gelatinase AGelatinase A (vertaling onbekend)A secreted endopeptidase homologous with INTERSTITIAL COLLAGENASE, but which possesses an additional fibronectin-like domain. EC 3.4.24.24.D020780D08.586.277.656.300.480.252.445Gelatinase BGelatinase B (vertaling onbekend)An endopeptidase that is structurally similar to GELATINASE A. It degrades types I and V GELATIN and types IV and V COLLAGEN. EC 3.4.24.35.D007339D08.586.277.656.300.480.300InsulysinInsulysin (vertaling onbekend)An enzyme the catalyzes the degradation of insulin, glucagon and other polypeptides. It is inhibited by bacitracin, chelating agents EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not phosphoramidon. (Eur J BiocD008248D08.586.277.656.300.480.452LysostaphinLysostaphin (vertaling onbekend)A 25 kD peptidase produced by Staphylococcus simulans which cleaves a glycine-glcyine bond unique to an inter-peptide cross-bridge of the STAPHYLOCOCCUS AUREUS cell wall. EC 3.4.24.75.D020782D08.586.277.656.300.480.525Matrix MetalloproteinasesMatrix Metalloproteinases (vertaling onbekend)A family of zinc-dependent METALLOENDOPROTEINASES that are involved in the degradation of EXTRACELLULAR MATRIX components. EC 3.4.24.-.D020778D08.586.277.656.300.480.525.352Gelatinase AGelatinase A (vertaling onbekend)A secreted endopeptidase homologous with INTERSTITIAL COLLAGENASE, but which possesses an additional fibronectin-like domain. EC 3.4.24.24.D020780D08.586.277.656.300.480.525.360Gelatinase BGelatinase B (vertaling onbekend)An endopeptidase that is structurally similar to GELATINASE A. It degrades types I and V GELATIN and types IV and V COLLAGEN. EC 3.4.24.35.D020781D08.586.277.656.300.480.525.451Interstitial CollagenaseInterstitial Collagenase (vertaling onbekend)A member of the metalloproteinase family of enzymes that is principally responsible for cleaving fibrillar collagen. It can degrade interstitial collagens, types I, II and III. EC 3.4.24.7.D020783D08.586.277.656.300.480.525.505MatrilysinMatrilysin (vertaling onbekend)The smallest member of the MATRIX METALLOPROTEINASES. It plays a role in tumor progression. EC 3.4.24.23.D020784D08.586.277.656.300.480.525.615Neutrophil CollagenaseNeutrophil Collagenase (vertaling onbekend)A member of the MATRIX METALLOPROTEINASES that cleaves triple-helical collagens types I, II, and III. EC 3.4.24.34.D019278D08.586.277.656.300.480.525.810Stromelysin 1Stromelysin 1 (vertaling onbekend)An extracellular endopeptidase of vertebrate tissues similar to INTERSTITIAL COLLAGENASE. It digests proteoglycan, fibronectin, collagen types III, IV, V, and IX, and activates procollagenase. (Enzyme Nomenclature, 1992) EC 3.4.24.17.D015260D08.586.277.656.300.480.600NeprilysinNeprilysin (vertaling onbekend)Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well asD011348D08.586.277.656.300.480.664Procollagen N-EndopeptidaseProcollagen N-Endopeptidase (vertaling onbekend)An extracellular endopeptidase which excises a block of peptides at the amino terminal, nonhelical region of the procollagen molecule with the formation of collagen. Absence or deficiency of the enzyme causes accumulation of procollagen which results in tD011402D08.586.277.656.300.480.680PronasePronase (vertaling onbekend)A proteolytic enzyme obtained from Streptomyces griseus.D013820D08.586.277.656.300.480.827ThermolysinThermolysin (vertaling onbekend)A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.D012697D08.586.277.656.300.760Serine EndopeptidasesSerine Endopeptidases (vertaling onbekend)Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis. EC 3.4.21.D000176D08.586.277.656.300.760.030AcrosinAcrosin (vertaling onbekend)A trypsin-like enzyme of spermatozoa which is not inhibited by alpha 1 antitrypsin.D002918D08.586.277.656.300.760.176ChymotrypsinChymotrypsin (vertaling onbekend)A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.D011415D08.586.277.656.300.760.198Complement Factor BComplement Factor B (vertaling onbekend)A glycine-rich, heat-labile beta-glycoprotein found in blood. It is a proactivator of complement 3 in the alternate pathway of complement activation. Factor B is converted by Factor D to COMPLEMENT 3 CONVERTASE. EC 3.4.21.47.D011416D08.586.277.656.300.760.200Complement Factor DComplement Factor D (vertaling onbekend)A serum protein which during the alternate pathway of complement activation converts the inactive factor B to COMPLEMENT 3 CONVERTASE. EC 3.4.21.46.D017244D08.586.277.656.300.760.210Complement Factor IComplement Factor I (vertaling onbekend)Serine proteinase that acts on iC3b (inactivated complement 3b) to cleave it into C3c and C3dg with the help of a trypsin-like proteolytic enzyme. Complement factor I was formerly called KAF, C3bINF, or enzyme 3b inactivator. EC 3.4.21.45.D019286D08.586.277.656.300.760.247Endopeptidase KEndopeptidase K (vertaling onbekend)An enzyme that catalyzes the hydrolysis of keratin, and of other proteins with subtilisin-like specificity. It hydrolyses peptide amides. Endopeptidase K is from the mold Tritirachium album Limber. (Enzyme Nomenclature, 1992) EC 3.4.21.64.D004765D08.586.277.656.300.760.284EnteropeptidaseEnteropeptidase (vertaling onbekend)A specialized proteolytic enzyme secreted by intestinal cells. It converts TRYPSINOGEN into its active form TRYPSIN by removing the N-terminal peptide. EC 3.4.21.9.D015942D08.586.277.656.300.760.300Factor VIIaFactor VIIa (vertaling onbekend)Activated form of factor VII. Factor VIIa activates factor X in the extrinsic pathway of blood coagulation.D015949D08.586.277.656.300.760.310Factor IXaFactor IXa (vertaling onbekend)Activated form of factor IX. This activation can take place via the intrinsic pathway by the action of factor XIa and calcium, or via the extrinsic pathway by the action of factor VIIa, thromboplastin, and calcium. Factor IXa serves to activate factor X tD015951D08.586.277.656.300.760.315Factor XaFactor Xa (vertaling onbekend)Activated form of factor X that participates in both the intrinsic and extrinsic pathways of blood coagulation. It catalyzes the conversion of prothrombin to thrombin in conjunction with other cofactors.D015945D08.586.277.656.300.760.320Factor XIaFactor XIa (vertaling onbekend)Activated form of factor XI. In the intrinsic pathway, Factor XI is activated to XIa by factor XIIa in the presence of cofactor HMWK; (HIGH MOLECULAR WEIGHT KININOGEN). Factor XIa then activates factor IX to factor IXa in the presence of calcium.D015956D08.586.277.656.300.760.324Factor XIIaFactor XIIa (vertaling onbekend)Activated form of factor XII. In the initial event in the intrinsic pathway of blood coagulation, kallikrein (with cofactor HIGH MOLECULAR WEIGHT KININOGEN) cleaves factor XII to XIIa. Factor XIIa is then further cleaved by kallikrein, plasmin, and trypsiD007610D08.586.277.656.300.760.442KallikreinsKallikreins (vertaling onbekend)Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increases vascular permeability and affects smooth muscle. They act as infertility agents in mD020842D08.586.277.656.300.760.442.700Plasma KallikreinPlasma Kallikrein (vertaling onbekend)A peptidohydrolytic enzyme that is formed from PREKALLIKREIN by FACTOR XIIA. It activates FACTOR XII; FACTOR VII; and PLASMINOGEN. It is selective for both ARGININE and to a lesser extent LYSINE bonds. EC 3.4.21.34.D011288D08.586.277.656.300.760.442.725PrekallikreinPrekallikrein (vertaling onbekend)A plasma protein which is the precursor of kallikrein. Plasma that is deficient in prekallikrein has been found to be abnormal in thromboplastin formation, kinin generation, evolution of a permeability globulin, and plasmin formation. The absence of prekaD017430D08.586.277.656.300.760.442.750Prostate-Specific AntigenProstate-Specific Antigen (vertaling onbekend)A glycoprotein that is a kallikrein-like serine proteinase and an esterase, produced by epithelial cells of both normal and malignant prostate tissue. It is an important marker for the diagnosis of prostate cancer.D020840D08.586.277.656.300.760.442.875Tissue KallikreinsTissue Kallikreins (vertaling onbekend)A family of trpysin-like SERINE ENDOPEPTIDASES that are expressed in a variety of cell types including human prostate epithelial cells. They are formed from tissue prokallikrein by action with TRYPSIN. They are highly similar to PROSTATE-SPECIFIC ANTIGEN.D010196D08.586.277.656.300.760.560Pancreatic ElastasePancreatic Elastase (vertaling onbekend)A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.D019272D08.586.277.656.300.760.560.500Leukocyte ElastaseLeukocyte Elastase (vertaling onbekend)An enzyme that catalyzes the hydrolysis of proteins, including elastin. It cleaves preferentially bonds at the carboxyl side of Ala and Val, with greater specificity for Ala. EC 3.4.21.37.D005341D08.586.277.656.300.760.625PlasminPlasmin (vertaling onbekend)A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction oD010960D08.586.277.656.300.760.635Plasminogen ActivatorsPlasminogen Activators (vertaling onbekend)A heterogeneous group of proteolytic enzymes that convert plasminogen to plasmin. They are concentrated in the lysosomes of most cells and in the vascular endothelium, particularly in the vessels of the microcirculation. EC 3.4.21.-.D016255D08.586.277.656.300.760.635.075AnistreplaseAnistreplase (vertaling onbekend)An acylated inactive complex of streptokinase and human lysine-plasminogen. After injection, the acyl group is slowly hydrolyzed, producing an activator that converts plasminogen to plasmin, thereby initiating fibrinolysis. Its half-life is about 90 minutD011402D08.586.277.656.300.760.680PronasePronase (vertaling onbekend)A proteolytic enzyme obtained from Streptomyces griseus.D013381D08.586.277.656.300.760.787SubtilisinsSubtilisins (vertaling onbekend)A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-D020860D08.586.277.656.300.760.787.805SubtilisinSubtilisin (vertaling onbekend)A serine endopeptidase isolated from Bacillus subtilis. It hydrolyzes proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. It also hydrolyzes peptide amides. (From Enzyme Nomenclature, 1992) EC 3.4.21.62D013917D08.586.277.656.300.760.855ThrombinThrombin (vertaling onbekend)An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN.D010959D08.586.277.656.300.760.875Tissue Plasminogen ActivatorTissue Plasminogen Activator (vertaling onbekend)A proteolytic enzyme in the serine protease family found in many tissues which converts PLASMINOGEN to PLASMIN. It has fibrin-binding activity and is immunologically different from URINARY PLASMINOGEN ACTIVATOR. The primary sequence, composed of 527 aminoD014357D08.586.277.656.300.760.895TrypsinTrypsin (vertaling onbekend)A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.D014568D08.586.277.656.300.760.910Urinary Plasminogen ActivatorUrinary Plasminogen Activator (vertaling onbekend)A proteolytic enzyme that converts plasminogen to plasmin where the preferential cleavage is between arginine and valine. It was isolated originally from human urine, but is found in most tissues of most vertebrates. EC 3.4.21.73.D020791D08.586.277.656.300.760.955Venombin AVenombin A (vertaling onbekend)A thrombin-like enzyme from the venom of snakes of the viper/rattlesnake group. Species variants of the enzyme include ANCROD (Agkistrodon rhodostoma (Malayan pit viper)); BATROXOBIN from Bothrops atrox; and crotalase from Crotalus adamanteus (Eastern diaD000721D08.586.277.656.300.760.955.060AncrodAncrod (vertaling onbekend)An enzyme fraction from the venom of the Malayan pit viper, Agkistrodon rhodostoma. It catalyzes the hydrolysis of a number of amino acid esters and a limited proteolysis of fibrinogen. It is used clinically to produce controlled defibrination in patientsD012103D08.586.277.656.300.760.955.135BatroxobinBatroxobin (vertaling onbekend)A proteolytic enzyme obtained from the venom of fer-de-lance (Bothrops atrox). It is used as a plasma clotting agent for fibrinogen and for the detection of fibrinogen degradation products. The presence of heparin does not interfere with the clotting testD013300D08.586.277.656.300.775StreptokinaseStreptokinase (vertaling onbekend)Streptococcal fibrinolysin . An enzyme produced by hemolytic streptococci. It hydrolyzes amide linkages and serves as an activator of plasminogen. It is used in thrombolytic therapy and is used also in mixtures with streptodornase (STREPTODORNASE AND STRED016255D08.586.277.656.300.775.075AnistreplaseAnistreplase (vertaling onbekend)An acylated inactive complex of streptokinase and human lysine-plasminogen. After injection, the acyl group is slowly hydrolyzed, producing an activator that converts plasminogen to plasmin, thereby initiating fibrinolysis. Its half-life is about 90 minutD013299D08.586.277.656.300.775.900Streptodornase and StreptokinaseStreptodornase and Streptokinase (vertaling onbekend)A mixture of the enzymes (streptokinase and streptodornase) produced by hemolytic streptococci. It is used topically on surface lesions and by instillation in closed body cavities to remove clotted blood or fibrinous or purulent accumulations. It is also D020689D08.586.277.656.350ExopeptidasesExopeptidases (vertaling onbekend)A sub-subclass of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains. Exopeptidases are further divided into AMINOPEPTIDASES; EC 3.4.11; DIPEPTIDASES; EC 3.4.13; DIPEPTIDYL PEPTIDASES & tripeptidyl peptidases, EC 3.4.14; peptidyl-dipD000626D08.586.277.656.350.100AminopeptidasesAminopeptidases (vertaling onbekend)A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.D000593D08.586.277.656.350.100.150Amino Acid NaphthylamidasesAmino Acid Naphthylamidases (vertaling onbekend)blaD007936D08.586.277.656.350.100.150.400Leucyl-beta-NaphthylamidaseLeucyl-beta-Naphthylamidase (vertaling onbekend)An aminopeptidase frequently used to test for LEUCYL AMINOPEPTIDASE activity. It also hydrolyzes naphthylamides of leucine. EC 3.4.11.-.D018826D08.586.277.656.350.100.160Antigens, CD13Antigens, CD13 (vertaling onbekend)Glycoproteins expressed on human granulocyte-monocyte progenitor colony forming units (CFU-GM) and their more differentiated progeny. The enzymes are also found in a large number of tissues, often associated with membranes. EC 3.4.11.2D010122D08.586.277.656.350.100.235Cystinyl AminopeptidaseCystinyl Aminopeptidase (vertaling onbekend)A zinc-containing sialoglycoprotein that is used to study aminopeptidase activity in the pathogenesis of hypertension. EC 3.4.11.3.D007931D08.586.277.656.350.100.511Leucyl AminopeptidaseLeucyl Aminopeptidase (vertaling onbekend)A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tisD007936D08.586.277.656.350.100.511.400Leucyl-beta-NaphthylamidaseLeucyl-beta-Naphthylamidase (vertaling onbekend)An aminopeptidase frequently used to test for LEUCYL AMINOPEPTIDASE activity. It also hydrolyzes naphthylamides of leucine. EC 3.4.11.-.D002268D08.586.277.656.350.245CarboxypeptidasesCarboxypeptidases (vertaling onbekend)Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue. They are further divided based on their catalytic mechanism into serine-type carboxypeptidases EC 3.4.16; metallocarboxypeptidases, EC 3.4.17; and cysteine-typD025901D08.586.277.656.350.245.224Carboxypeptidase UCarboxypeptidase U (vertaling onbekend)A metallocarboxypeptidase that removes C-terminal lysine and arginine from biologically active peptides and proteins thereby regulating their activity. It is a zinc enzyme with no preference shown for lysine over arginine. Pro-carboxypeptidase U in human D001121D08.586.277.656.350.245.450Lysine CarboxypeptidaseLysine Carboxypeptidase (vertaling onbekend)A metallocarboxypeptidase that removes C-terminal basic amino acid from peptides and proteins, with preference shown for lysine over arginine. It is a plasma zinc enzyme that inactivates bradykinin and anaphylatoxins.D002267D08.586.277.656.350.245.500Muramoylpentapeptide CarboxypeptidaseMuramoylpentapeptide Carboxypeptidase (vertaling onbekend)Enzyme produced by Streptomyces strain R61 which catalyzes the peptide cross-linking of nascent cell-wall peptidoglycan. EC 3.4.17.8.D004150D08.586.277.656.350.297DipeptidasesDipeptidases (vertaling onbekend)EXOPEPTIDASES that specifically act on dipeptides. EC 3.4.13.D004152D08.586.277.656.350.350Dipeptidyl PeptidasesDipeptidyl Peptidases (vertaling onbekend)Enzymes which cleave dipeptides from the amino terminal of a polypeptide. Dipeptidyl peptidase I, II, III, IV are known. They hydrolyze the beta-naphthylamides of glycine-arginine, lysine-alanine, arginine-arginine and glycine-proline, respectively. DIPEPD018819D08.586.277.656.350.350.126Antigens, CD26Antigens, CD26 (vertaling onbekend)Cell-surface glycoproteins and serine protease, also known as dipeptidyl-peptidase IV, that play a role in T-lymphocyte activation. CD26 binds to adenosine deaminase on the T-cell surface. EC 3.4.14.5D020789D08.586.277.656.350.350.375Dipeptidyl Peptidase IDipeptidyl Peptidase I (vertaling onbekend)A cysteine-type peptidase that is CHLORINE dependent and functions maximally at acidic pHs. At neutral pH, it polymerizes esters, aryl- and dipeptide amides. EC 3.4.14.1.D011623D08.586.277.656.350.410gamma-Glutamyl Hydrolasegamma-Glutamyl Hydrolase (vertaling onbekend)Catalyzes the hydrolysis of pteroylpolyglutamic acids in gamma linkage to pterolylmonoglutamic acid and free glutamic acid. EC 3.4.19.9.D007703D08.586.277.656.350.700Peptidyl-Dipeptidase APeptidyl-Dipeptidase A (vertaling onbekend)A peptidyl-dipeptidase that catalyzes the release of a C-terminal dipeptide, -Xaa-*-Xbb-Xcc, when neither Xaa nor Xbb is Pro. It is a Cl(-)-dependent, zinc glycoprotein that is generally membrane-bound and active at neutral pH. It may also have endopeptidD011751D08.586.277.656.350.730Pyroglutamyl-Peptidase IPyroglutamyl-Peptidase I (vertaling onbekend)An enzyme that catalyzes the release of a N-terminal pyroglutamyl group from a polypeptide provided the next residue is not proline. It is inhibited by thiol-blocking reagents and occurs in mammalian tissues, microorganisms, and plants. (From Enzyme NomenD011938D08.586.277.656.850Rec A ProteinRec A Protein (vertaling onbekend)Protein from E.coli rec gene. Catalyzes the ATP-driven exchange of DNA strands in genetic recombination. The product of the reaction consists of a duplex and a displaced single-stranded loop which has the shape of the letter D and is therefore called a D-D014512D08.586.277.913UreohydrolasesUreohydrolases (vertaling onbekend)blaD001119D08.586.277.913.292ArginaseArginase (vertaling onbekend)A ureahydrolase that catalyzes the hydrolysis of arginine or canavanine to yield L-ORNITHINE and urea. Deficiency of this enzyme causes HYPERARGININEMIA. EC 3.5.3.1.D007527D08.586.348IsoenzymesIsoenzymes (vertaling onbekend)One of various structurally related forms of an enzyme, each having the same mechanism but with differing chemical, physical, or immunological characteristics.D007535D08.586.399IsomerasesIsomerases (vertaling onbekend)A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5D019745D08.586.399.325cis-trans-Isomerasescis-trans-Isomerases (vertaling onbekend)Enzymes that catalyze the rearrangement of geometry about double bonds. EC 5.2.D019696D08.586.399.325.500Peptidylprolyl IsomerasePeptidylprolyl Isomerase (vertaling onbekend)An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8.D020104D08.586.399.325.500.400ImmunophilinsImmunophilins (vertaling onbekend)Members of a family of highly conserved proteins which are all cis-trans peptidyl-prolyl isomerases (PEPTIDYLPROLYL ISOMERASE). They bind the immunosuppressant drugs CYCLOSPORINE; TACROLIMUS and SIROLIMUS. They possess rotomase activity, which is inhibiteD021983D08.586.399.325.500.400.300CyclophilinsCyclophilins (vertaling onbekend)A family of peptidyl-prolyl cis-trans isomerases that bind to CYCLOSPORINS and regulate the IMMUNE SYSTEM. EC 5.2.1.-D021984D08.586.399.325.500.400.300.500Cyclophilin ACyclophilin A (vertaling onbekend)A 17 KD cytoplasmic PEPTIDYLPROLYL ISOMERASE involved in immunoregulation. It is a member of the cyclophilin family of proteins that binds to CYCLOSPORINE. EC 5.2.1.-D022021D08.586.399.325.500.400.700Tacrolimus Binding ProteinsTacrolimus Binding Proteins (vertaling onbekend)A family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-D022061D08.586.399.325.500.400.700.500Tacrolimus Binding Protein 1ATacrolimus Binding Protein 1A (vertaling onbekend)A 12 KD tacrolimus binding protein that is found associated with and may modulate the function of calcium release channels. It is a peptidyl-prolyl cis/trans isomerase which is inhibtied by both tacrolimus (commonly called FK506) and SIROLIMUS. EC 5.2.1.-D004265D08.586.399.340DNA HelicasesDNA Helicases (vertaling onbekend)Proteins that promote unwinding of duplex DNA during replication by binding cooperatively to single-stranded regions of DNA or to short regions of duplex DNA that are undergoing transient opening. EC 5.99.-.D026942D08.586.399.403DNA TopoisomerasesDNA Topoisomerases (vertaling onbekend)Enzymes that regulate the topology of DNA by actions such as breaking, relaxing, passing, and rejoining strands of DNA in cells. These enzymes are important components of the DNA replication system. They are classified by their substrate specificities. DND004264D08.586.399.403.483DNA Topoisomerases, Type IDNA Topoisomerases, Type I (vertaling onbekend)DNA TOPOISOMERASES that catalyze ATP-independent breakage of one of the two strands of DNA, passage of the unbroken strand through the break, and rejoining of the broken strand. DNA Topoisomerases, Type I enzymes reduce the topological stress in the DNA sD027847D08.586.399.403.483.249DNA Topoisomerases, Type I, ArchaealDNA Topoisomerases, Type I, Archaeal (vertaling onbekend)Archaeal enzymes of the DNA TOPOISOMERASES TYPE I class that catalyze ATP-independent breakage of one of the two strands of DNA, passage of the unbroken strand through the break, and rejoining of the broken strand. These archaeal enzymes reduce the topoloD027024D08.586.399.403.483.300DNA Topoisomerases, Type I, BacterialDNA Topoisomerases, Type I, Bacterial (vertaling onbekend)Bacterial enzymes of the DNA TOPOISOMERASES TYPE I class that catalyze ATP-independent breakage of one of the two strands of DNA, passage of the unbroken strand through the break, and rejoining of the broken strand. These bacterial enzymes reduce the topoD027025D08.586.399.403.483.500DNA Topoisomerases, Type I, EukaryoticDNA Topoisomerases, Type I, Eukaryotic (vertaling onbekend)Eukaryotic enzymes of the DNA TOPOISOMERASES TYPE I class that catalyze ATP-independent breakage of one of the two strands of DNA, passage of the unbroken strand through the break, and rejoining of the broken strand. These eukaryotic enzymes reduce the toD004250D08.586.399.403.741DNA Topoisomerases, Type IIDNA Topoisomerases, Type II (vertaling onbekend)DNA TOPOISOMERASES that catalyze ATP-dependent breakage of both strands of DNA, passage of the unbroken strands through the breaks, and rejoining of the broken strands. These enzymes bring about relaxation of the supercoiled DNA and resolution of a knotteD027921D08.586.399.403.741.249DNA Topoisomerases, Type II, ArchaealDNA Topoisomerases, Type II, Archaeal (vertaling onbekend)Archaeal enzymes of the DNA TOPOISOMERASES, TYPE II class that catalyze ATP-dependent breakage of both strands of DNA, passage of the unbroken strands through the breaks, and rejoining of the broken strands. These enzymes bring about relaxation of the supD027061D08.586.399.403.741.300DNA Topoisomerases, Type II, BacterialDNA Topoisomerases, Type II, Bacterial (vertaling onbekend)Bacterial enzymes of the DNA TOPOISOMERASES TYPE II class that catalyze ATP-dependent breakage of both strands of DNA, passage of the unbroken strands through the breaks, and rejoining of the broken strands. These enzymes bring about relaxation of the supD027081D08.586.399.403.741.300.500DNA GyraseDNA Gyrase (vertaling onbekend)A bacterial DNA topoisomerase II that catalyzes ATP-dependent breakage of both strands of DNA, passage of the unbroken strands through the breaks, and rejoining of the broken strands. Gyrase binds to DNA as a heterotetramer consisting two A and two B subuD027101D08.586.399.403.741.300.750DNA Topoisomerase IVDNA Topoisomerase IV (vertaling onbekend)A bacterial DNA topoisomerase II that catalyzes ATP-dependent breakage of both strands of DNA, passage of the unbroken strands through the breaks, and rejoining of the broken strands. Topoisomerase IV binds to DNA as a heterotetramer consisting 2 parC andD029081D08.586.399.403.741.500DNA Topoisomerases, Type II, EukaryoticDNA Topoisomerases, Type II, Eukaryotic (vertaling onbekend)Eukaryotic enzymes of the DNA TOPOISOMERASES, TYPE II class that catalyze ATP-dependent breakage of both strands of DNA, passage of the unbroken strands through the breaks, and rejoining of the broken strands. These enzymes bring about relaxation of the D019753D08.586.399.430Intramolecular LyasesIntramolecular Lyases (vertaling onbekend)Enzymes of the isomerase class that catalyze reactions in which a group can be regarded as eliminated from one part of a molecule, leaving a double bond, while remaining covalently attached to the molecule. (From Enzyme Nomenclature, 1992) EC 5.5.D007296D08.586.399.430.500myo-Inositol-1-Phosphate Synthasemyo-Inositol-1-Phosphate Synthase (vertaling onbekend)An enzyme that catalyzes the formation of myo-inositol-1-phosphate from glucose-6-phosphate in the presence of NAD. EC 5.5.1.4.D019746D08.586.399.475Intramolecular OxidoreductasesIntramolecular Oxidoreductases (vertaling onbekend)Enzymes of the isomerase class that catalyze the oxidation of one part of a molecule with a corresponding reduction of another part of the same molecule. They include enzymes converting aldoses to ketoses (ALDOSE-KETOSE ISOMERASES), enzymes shifting a carD019747D08.586.399.475.200Aldose-Ketose IsomerasesAldose-Ketose Isomerases (vertaling onbekend)Enzymes that catalyze the interconversion of aldoses and ketoses. EC 5.3.1.D005956D08.586.399.475.200.350Glucose-6-Phosphate IsomeraseGlucose-6-Phosphate Isomerase (vertaling onbekend)An enzyme that catalyzes the reversible interconversion of glucose 6-phosphate and fructose 6-phosphate, and is a part of the glycolytic and gluconeogenic pathways. Deficiency of the enzyme, an autosomal recessive trait, results in liver glycogenesis and D008359D08.586.399.475.200.550Mannose-6-Phosphate IsomeraseMannose-6-Phosphate Isomerase (vertaling onbekend)An enzyme that catalyzes the reversible isomerization of D-mannose-6-phosphate to form D-fructose-6-phosphate, an important step in glycolysis. EC 5.3.1.8.D014305D08.586.399.475.200.775Triose-Phosphate IsomeraseTriose-Phosphate Isomerase (vertaling onbekend)An enzyme that catalyzes reversibly the conversion of D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate. A deficiency in humans causes nonspherocytic hemolytic disease (ANEMIA, HEMOLYTIC, CONGENITAL NONSPHEROCYTIC). EC 5.3.1.1.D019748D08.586.399.475.400Carbon-Carbon Double Bond IsomerasesCarbon-Carbon Double Bond Isomerases (vertaling onbekend)Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to another within the same molecule. EC 5.3.3.D013251D08.586.399.475.400.700Steroid IsomerasesSteroid Isomerases (vertaling onbekend)Enzymes that catalyze the transposition of double bond(s) in a steroid molecule. EC 5.3.3.D019749D08.586.399.475.800Sulfur-Sulfur Bond IsomerasesSulfur-Sulfur Bond Isomerases (vertaling onbekend)Enzymes that catalyze the transposition of a sulfur-sulfur bond. EC 5.3.4.D019704D08.586.399.475.800.550Protein Disulfide-IsomeraseProtein Disulfide-Isomerase (vertaling onbekend)An enzyme that catalyzes the rearrangement of disulfide bonds within proteins during folding. It is a monomer identical to one of the subunits of PROCOLLAGEN-PROLINE DIOXYGENASE. (From Dorland, 28th ed) EC 5.3.4.1.D013930D08.586.399.475.900Thromboxane-A SynthaseThromboxane-A Synthase (vertaling onbekend)An enzyme found predominantly in platelet microsomes. It catalyzes the conversion of PGG(2) and PGH(2) (prostaglandin endoperoxides) to thromboxane A2. EC 5.3.99.5.D019751D08.586.399.520Intramolecular TransferasesIntramolecular Transferases (vertaling onbekend)Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.D015072D08.586.399.520.1002-Acetolactate Mutase2-Acetolactate Mutase (vertaling onbekend)An enzyme involved in the biosynthesis of isoleucine and valine. It converts 2-acetolactate into 3-hydroxy-2-oxo-isovalerate. Also acts on 2-hydroxy-2-acetobutyrate to form 2-hydroxy-2-oxo-3-methylvalerate. EC 5.4.99.3.D002826D08.586.399.520.250Chorismate MutaseChorismate Mutase (vertaling onbekend)An isomerase that catalyzes the conversion of chorismic acid to prephenic acid. EC 5.4.99.5.D011302D08.586.399.520.250.500Prephenate DehydratasePrephenate Dehydratase (vertaling onbekend)An enzyme that catalyzes the conversion of prephenate to phenylpyruvate with the elimination of water and carbon dioxide. In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthD011303D08.586.399.520.250.750Prephenate DehydrogenasePrephenate Dehydrogenase (vertaling onbekend)An enzyme that catalyzes the conversion of prephenate to p-hydroxyphenylpyruvate in the presence of NAD. In the enteric bacteria, this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of tyrosineD008765D08.586.399.520.625Methylmalonyl-CoA MutaseMethylmalonyl-CoA Mutase (vertaling onbekend)An enzyme that catalyzes the conversion of methylmalonyl-CoA to succinyl-CoA by transfer of the carbonyl group. It requires a cobamide coenzyme. A block in this enzymatic conversion leads to the metabolic disease, methylmalonic aciduria. EC 5.4.99.2.D017875D08.586.399.520.750Phosphotransferases (Phosphomutases)Phosphotransferases (Phosphomutases) (vertaling onbekend)A group of enzymes that catalyze an intramolecular transfer of a phosphate group. It has been shown in some cases that the enzyme has a functional phosphate group, which can act as the donor. These were previously listed under PHOSPHOTRANSFERASES (EC 2.7.D001731D08.586.399.520.750.250Bisphosphoglycerate MutaseBisphosphoglycerate Mutase (vertaling onbekend)An enzyme that catalyzes the transfer of phosphate from C-3 of 1,3-diphosphoglycerate to C-2 of 3-phosphoglycerate, forming 2,3-diphosphoglycerate. EC 5.4.2.4.D010733D08.586.399.520.750.625PhosphoglucomutasePhosphoglucomutase (vertaling onbekend)An enzyme that catalyzes the conversion of alpha D-glucose 1-phosphate to alpha D-glucose 6-phosphate. EC 5.4.2.2.D010736D08.586.399.520.750.700Phosphoglycerate MutasePhosphoglycerate Mutase (vertaling onbekend)An enzyme that catalyzes the conversion of 2-phospho-D-glycerate to 3-phospho-D-glycerate. EC 5.4.2.1.D019998D08.586.399.894Racemases and EpimerasesRacemases and Epimerases (vertaling onbekend)Enzymes that catalyze inversion of the configuration around an asymmetric carbon in a substrate having one (racemase) or more (epimerase) center(s) of asymmetry. (Dorland, 28th ed) EC 5.1.D000591D08.586.399.894.200Amino Acid IsomerasesAmino Acid Isomerases (vertaling onbekend)Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.D000411D08.586.399.894.200.200Alanine RacemaseAlanine Racemase (vertaling onbekend)A pyridoxal-phosphate protein that reversibly catalyzes the conversion of L-alanine to D-alanine. EC 5.1.1.1.D002238D08.586.399.894.500Carbohydrate EpimerasesCarbohydrate Epimerases (vertaling onbekend)Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.D014534D08.586.399.894.500.700UDPglucose 4-EpimeraseUDPglucose 4-Epimerase (vertaling onbekend)A necessary enzyme in the metabolism of galactose. It reversibly catalyzes the conversion of UDPglucose to UDPgalactose. NAD+ is an essential component for enzymatic activity. EC 5.1.3.2.D008025D08.586.464LigasesLigases (vertaling onbekend)A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.D019735D08.586.464.257Carbon-Carbon LigasesCarbon-Carbon Ligases (vertaling onbekend)Enzymes that catalyze the joining of two molecules by the formation of a carbon-carbon bond. These are the carboxylating enzymes and are mostly biotinyl-proteins. EC 6.4.D000103D08.586.464.257.050Acetyl-CoA CarboxylaseAcetyl-CoA Carboxylase (vertaling onbekend)A carboxylating enzyme that catalyzes the conversion of ATP, acetyl-CoA, and HCO3- to ADP, orthophosphate, and malonyl-CoA. It is a biotinyl-protein that also catalyzes transcarboxylation. The plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA D011766D08.586.464.257.500Pyruvate CarboxylasePyruvate Carboxylase (vertaling onbekend)A biotin-dependent enzyme belonging to the ligase family that catalyzes the addition of CARBON DIOXIDE to pyruvate. It is occurs in both plants and animals. Deficiency of this enzyme causes severe psychomotor retardation and ACIDOSIS, LACTIC in infants. ED019731D08.586.464.259Carbon-Nitrogen LigasesCarbon-Nitrogen Ligases (vertaling onbekend)Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.D000265D08.586.464.259.100Adenylosuccinate SynthaseAdenylosuccinate Synthase (vertaling onbekend)A carbon-nitrogen ligase. During purine ribonucleotide biosynthesis, this enzyme catalyzes the synthesis of adenylosuccinate from GTP; IMP; and aspartate with the formation of orthophosphate and GDP. EC 6.3.4.4.D019732D08.586.464.259.200Amide SynthasesAmide Synthases (vertaling onbekend)Enzymes that catalyze the joining of either ammonia or an amide with another molecule, in which the linkage is in the form of a carbon-nitrogen bond. EC 6.3.1.D001217D08.586.464.259.200.200Aspartate-Ammonia LigaseAspartate-Ammonia Ligase (vertaling onbekend)An enzyme that catalyzes the formation of asparagine from ammonia and aspartic acid, in the presence of ATP. EC 6.3.1.1.D005974D08.586.464.259.200.600Glutamate-Ammonia LigaseGlutamate-Ammonia Ligase (vertaling onbekend)An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and L-glutamine. It also acts more slowly on 4-methylene-L-glutamate. (From Enzyme Nomenclature, 1992) EC 6.3.1.2.D001124D08.586.464.259.300Argininosuccinate SynthaseArgininosuccinate Synthase (vertaling onbekend)An enzyme of the urea cycle that catalyzes the formation of argininosuccinic acid from citrulline and aspartic acid in the presence of ATP. Absence or deficiency of this enzyme causes the metabolic disease CITRULLINEMIA in humans. EC 6.3.4.5.D002222D08.586.464.259.350Carbamoyl-Phosphate Synthase (Ammonia)Carbamoyl-Phosphate Synthase (Ammonia) (vertaling onbekend)An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and ammonia. This enzyme is specific for arginine biosynthesis or the urea cycle. Absence or lack of this enzyme may cause CARBAMOYL-PHOSPHATE SYNTHASE I DEFICIENCY. ED019733D08.586.464.259.400Carbon-Nitrogen Ligases with Glutamine as Amide-N-DonorCarbon-Nitrogen Ligases with Glutamine as Amide-N-Donor (vertaling onbekend)Enzymes that catalyze the joining of glutamine-derived ammonia and another molecule. The linkage is in the form of a carbon-nitrogen bond. EC 6.3.5.D002223D08.586.464.259.400.300Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) (vertaling onbekend)An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and glutamine. This enzyme is important in the de novo biosynthesis of pyrimidines. EC 6.3.5.5.D005574D08.586.464.259.550Formate-Tetrahydrofolate LigaseFormate-Tetrahydrofolate Ligase (vertaling onbekend)An enzyme that catalyzes the formation of 10-formyltetrahydrofolate from formate and tetrahydrofolate in the presence of ATP. This enzyme has been found in pigeon liver, human erythrocytes and some microorganisms. EC 6.3.4.3.D010453D08.586.464.259.850Peptide SynthasesPeptide Synthases (vertaling onbekend)Enzymes that catalyze the joining of an acid and an amino acid by the formation of a carbon-nitrogen bond. EC 6.3.2.D005721D08.586.464.259.850.400Glutamate-Cysteine LigaseGlutamate-Cysteine Ligase (vertaling onbekend)One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of gamma-glutamylcysteine from glutamate and cysteine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.2.D005981D08.586.464.259.850.500Glutathione SynthaseGlutathione Synthase (vertaling onbekend)One of the enzymes active in the gamma-glutamyl cycle. It catalyzes the synthesis of glutathione from gamma-glutamylcysteine and glycine in the presence of ATP with the formation of ADP and orthophosphate. EC 6.3.2.3.D019729D08.586.464.263Carbon-Oxygen LigasesCarbon-Oxygen Ligases (vertaling onbekend)Enzymes that catalyze the joining of two molecules by the formation of a carbon-oxygen bond. EC 6.1.D000604D08.586.464.263.200Amino Acyl-tRNA LigasesAmino Acyl-tRNA Ligases (vertaling onbekend)A subclass of enzymes that acylate a specific RNA, TRANSFER with the corresponding amino acid. EC 6.1.1.D000412D08.586.464.263.200.050Alanine-tRNA LigaseAlanine-tRNA Ligase (vertaling onbekend)An enzyme that activates alanine with its specific transfer RNA. EC 6.1.1.7.D001126D08.586.464.263.200.100Arginine-tRNA LigaseArginine-tRNA Ligase (vertaling onbekend)An enzyme that activates arginine with its specific transfer RNA. EC 6.1.1.19.D001226D08.586.464.263.200.150Aspartate-tRNA LigaseAspartate-tRNA Ligase (vertaling onbekend)An enzyme that activates aspartic acid with its specific transfer RNA. EC 6.1.1.12.D005975D08.586.464.263.200.250Glutamate-tRNA LigaseGlutamate-tRNA Ligase (vertaling onbekend)An enzyme that activates glutamic acid with its specific transfer RNA. EC 6.1.1.17.D006032D08.586.464.263.200.350Glycine-tRNA LigaseGlycine-tRNA Ligase (vertaling onbekend)An enzyme that activates glycine with its specific transfer RNA. EC 6.1.1.14.D006643D08.586.464.263.200.400Histidine-tRNA LigaseHistidine-tRNA Ligase (vertaling onbekend)An enzyme that activates histidine with its specific transfer RNA. EC 6.1.1.21.D007533D08.586.464.263.200.450Isoleucine-tRNA LigaseIsoleucine-tRNA Ligase (vertaling onbekend)An enzyme that activates isoleucine with its specific transfer RNA. EC 6.1.1.5.D007935D08.586.464.263.200.500Leucine-tRNA LigaseLeucine-tRNA Ligase (vertaling onbekend)An enzyme that activates leucine with its specific transfer RNA. EC 6.1.1.4.D008250D08.586.464.263.200.550Lysine-tRNA LigaseLysine-tRNA Ligase (vertaling onbekend)An enzyme that activates lysine with its specific transfer RNA. EC 6.1.1.6.D008718D08.586.464.263.200.600Methionine-tRNA LigaseMethionine-tRNA Ligase (vertaling onbekend)An enzyme that activates methionine with its specific transfer RNA. EC 6.1.1.10.D010652D08.586.464.263.200.650Phenylalanine-tRNA LigasePhenylalanine-tRNA Ligase (vertaling onbekend)An enzyme that activates phenylalanine with its specific transfer RNA. EC 6.1.1.20.D012714D08.586.464.263.200.750Serine-tRNA LigaseSerine-tRNA Ligase (vertaling onbekend)An enzyme that activates serine with its specific transfer RNA. EC 6.1.1.11.D013914D08.586.464.263.200.800Threonine-tRNA LigaseThreonine-tRNA Ligase (vertaling onbekend)An enzyme that activates threonine with its specific transfer RNA. EC 6.1.1.3.D014369D08.586.464.263.200.850Tryptophan-tRNA LigaseTryptophan-tRNA Ligase (vertaling onbekend)An enzyme that activates tryptophan with its specific transfer RNA. EC 6.1.1.2.D014448D08.586.464.263.200.900Tyrosine-tRNA LigaseTyrosine-tRNA Ligase (vertaling onbekend)An enzyme that activates tyrosine with its specific transfer RNA. EC 6.1.1.1.D014637D08.586.464.263.200.950Valine-tRNA LigaseValine-tRNA Ligase (vertaling onbekend)An enzyme that activates valine with its specific transfer RNA. EC 6.1.1.9D019730D08.586.464.267Carbon-Sulfur LigasesCarbon-Sulfur Ligases (vertaling onbekend)Enzymes that catalyze the joining of two molecules by the formation of a carbon-sulfur bond. EC 6.2.D003066D08.586.464.267.500Coenzyme A LigasesCoenzyme A Ligases (vertaling onbekend)Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.D000106D08.586.464.267.500.200Acetate-CoA LigaseAcetate-CoA Ligase (vertaling onbekend)An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.D013389D08.586.464.267.500.600Succinate-CoA LigasesSuccinate-CoA Ligases (vertaling onbekend)Enzymes that catalyze the first step leading to the oxidation of succinic acid by the reversible formation of succinyl-CoA from succinate and CoA with the concomitant cleavage of ATP to ADP (EC 6.2.1.5) or GTP to GDP (EC 6.2.1.4) and orthophosphate. ItacoD011118D08.586.464.754Polynucleotide LigasesPolynucleotide Ligases (vertaling onbekend)Catalyze the joining of preformed ribonucleotides or deoxyribonucleotides in phosphodiester linkage during genetic processes. EC 6.5.1.D011088D08.586.464.754.600DNA LigasesDNA Ligases (vertaling onbekend)Poly(deoxyribonucleotide):poly(deoxyribonucleotide)ligases. Enzymes that catalyze the joining of preformed deoxyribonucleotides in phosphodiester linkage during genetic processes during repair of a single-stranded break in duplex DNA. The class includes bD011130D08.586.464.754.720RNA Ligase (ATP)RNA Ligase (ATP) (vertaling onbekend)An enzyme that catalyzes the conversion of linear RNA to a circular form by the transfer of the 5'-phosphate to the 3'-hydroxyl terminus. It also catalyzes the covalent joining of two polyribonucleotides in phosphodiester linkage. EC 6.5.1.3.D008190D08.586.520LyasesLyases (vertaling onbekend)A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.D019755D08.586.520.224Carbon-Carbon LyasesCarbon-Carbon Lyases (vertaling onbekend)Enzymes that catalyze the cleavage of a carbon-carbon bond by means other than hydrolysis or oxidation. This subclass contains the DECARBOXYLASES, the ALDEHYDE-LYASES, and the OXO-ACID-LYASES. EC 4.1.D000446D08.586.520.224.062Aldehyde-LyasesAldehyde-Lyases (vertaling onbekend)Enzymes that catalyze a reverse aldol condensation. A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). EC 4.1.2.D019406D08.586.520.224.062.10017 alpha-Hydroxyprogesterone Aldolase17 alpha-Hydroxyprogesterone Aldolase (vertaling onbekend)An enzyme of the lyase class that catalyzes the cleavage of the bond between carbons 17 and 20 in 17-alpha hydroxyprogesterone to form delta 4-androstene-3,17-dione, an androgen. It also catalyzes the conversion of 17 alpha-hydroxypregnenolone to dehydroeD010723D08.586.520.224.062.2502-Dehydro-3-Deoxyphosphoheptonate Aldolase2-Dehydro-3-Deoxyphosphoheptonate Aldolase (vertaling onbekend)An enzyme that catalyzes the formation of 7-phospho-2-keto-3-deoxy-D-arabinoheptonate from phosphoenolpyruvate and D-erythrose-4-phosphate. It is one of the first enzymes in the biosynthesis of tyrosine and phenylalanine. EC 4.1.12.15.D005634D08.586.520.224.062.400Fructose-Bisphosphate AldolaseFructose-Bisphosphate Aldolase (vertaling onbekend)An enzyme of the lyase class that catalyzes the cleavage of fructose 1,6-biphosphate to form dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. The enzyme also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins.D002262D08.586.520.224.125Carboxy-LyasesCarboxy-Lyases (vertaling onbekend)Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.D012437D08.586.520.224.125.050Adenosylmethionine DecarboxylaseAdenosylmethionine Decarboxylase (vertaling onbekend)An enzyme that catalyzes the decarboxylation of S-adenosyl-L-methionine to yield 5'-deoxy-(5'-),3-aminopropyl-(1), methylsulfonium salt. It is one of the enzymes responsible for the synthesis of spermidine from putrescine. EC 4.1.1.50.D001142D08.586.520.224.125.100Aromatic-L-Amino-Acid DecarboxylasesAromatic-L-Amino-Acid Decarboxylases (vertaling onbekend)An enzyme group with broad specificity. The enzymes decarboxylate a range of aromatic amino acids including dihydroxyphenylalanine (DOPA DECARBOXYLASE), tryptophan, and hydroxytryptophan. EC 4.1.1.28.D004296D08.586.520.224.125.100.500Dopa DecarboxylaseDopa Decarboxylase (vertaling onbekend)One of the AROMATIC-L-AMINO-ACID DECARBOXYLASES, this enzyme is responsible for the conversion of dopa to dopamine. It is of clinical importance in the treatment of Parkinson's disease. EC 4.1.1.28.D005968D08.586.520.224.125.250Glutamate DecarboxylaseGlutamate Decarboxylase (vertaling onbekend)A pyridoxal-phosphate protein that catalyzes the alpha-decarboxylation of L-glutamic acid to form gamma-aminobutyric acid and carbon dioxide. The enzyme is found in bacteria and in invertebrate and vertebrate nervous systems. It is the rate-limiting enzymD006640D08.586.520.224.125.300Histidine DecarboxylaseHistidine Decarboxylase (vertaling onbekend)An enzyme that catalyzes the decarboxylation of histidine to histamine and carbon dioxide. It requires pyridoxal phosphate in animal tissues, but not in microorganisms. EC 4.1.1.22.D007209D08.586.520.224.125.350Indole-3-Glycerol-Phosphate SynthaseIndole-3-Glycerol-Phosphate Synthase (vertaling onbekend)An enzyme in the tryptophan biosynthetic pathway. EC 4.1.1.48.D009955D08.586.520.224.125.425Ornithine DecarboxylaseOrnithine Decarboxylase (vertaling onbekend)A pyridoxal-phosphate protein, believed to be the rate-limiting compound in the biosynthesis of polyamines. It catalyzes the decarboxylation of ornithine to form putrescine, which is then linked to a propylamine moiety of decarboxylated S-adenosylmethioniD009964D08.586.520.224.125.450Orotidine-5'-Phosphate DecarboxylaseOrotidine-5'-Phosphate Decarboxylase (vertaling onbekend)Orotidine-5'-phosphate carboxy-lyase. Catalyzes the decarboxylation of orotidylic acid to yield uridylic acid in the final step of the pyrimidine nucleotide biosynthesis pathway. EC 4.1.1.23.D019764D08.586.520.224.125.500Phosphoenolpyruvate Carboxykinase (ATP)Phosphoenolpyruvate Carboxykinase (ATP) (vertaling onbekend)An enzyme of the lyase class that catalyzes the conversion of ATP and oxaloacetate to ADP, phosphoenolpyruvate, and carbon dioxide. The enzyme is found in some bacteria, yeast, and Trypanosoma, and is important for the photosynthetic assimilation of carboD010729D08.586.520.224.125.550Phosphoenolpyruvate Carboxykinase (GTP)Phosphoenolpyruvate Carboxykinase (GTP) (vertaling onbekend)An enzyme of the lyase class that catalyzes the conversion of GTP and oxaloacetate to GDP, phosphoenolpyruvate, and carbon dioxide. This reaction is part of gluconeogenesis in the liver. The enzyme occurs in both the mitochondria and cytosol of mammalian D010730D08.586.520.224.125.650Phosphoenolpyruvate CarboxylasePhosphoenolpyruvate Carboxylase (vertaling onbekend)An enzyme with high affinity for carbon dioxide. It catalyzes irreversibly the formation of oxaloacetate from phosphoenolpyruvate and carbon dioxide. This fixation of carbon dioxide in several bacteria and some plants is the first step in the biosynthesisD011767D08.586.520.224.125.750Pyruvate DecarboxylasePyruvate Decarboxylase (vertaling onbekend)Catalyzes the decarboxylation of an alpha keto acid to an aldehyde and carbon dioxide. Thiamine pyrophosphate is an essential cofactor. In lower organisms, which ferment glucose to ethanol and carbon dioxide, the enzyme irreversibly decarboxylates pyruvatD012273D08.586.520.224.125.800Ribulose-Bisphosphate CarboxylaseRibulose-Bisphosphate Carboxylase (vertaling onbekend)A copper protein that catalyzes the formation of 2 moles of 3-phosphoglycerate from ribulose 1,5-biphosphate in the presence of carbon dioxide. It utilizes oxygen instead of carbon dioxide to form 2-phosphoglycollate and 3-phosphoglycerate. EC 4.1.1.39.D014445D08.586.520.224.125.875Tyrosine DecarboxylaseTyrosine Decarboxylase (vertaling onbekend)A pyridoxal-phosphate protein that catalyzes the conversion of L-tyrosine to tyramine and carbon dioxide. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine. (From Enzyme Nomenclature, 1992) EC 4.1.1.25.D014575D08.586.520.224.125.900Uroporphyrinogen DecarboxylaseUroporphyrinogen Decarboxylase (vertaling onbekend)One of the enzymes active in heme biosynthesis. It catalyzes the decarboxylation of uroporphyrinogen III to coproporphyrinogen III by the conversion of four acetic acid groups to four methyl groups. EC 4.1.1.37.D004255D08.586.520.224.187Deoxyribodipyrimidine Photo-LyaseDeoxyribodipyrimidine Photo-Lyase (vertaling onbekend)An enzyme that catalyzes the reactivation by light of UV-irradiated DNA. It breaks two carbon-carbon bonds in pyrimidine dimers in DNA. EC 4.1.99.3.D007652D08.586.520.224.600Oxo-Acid-LyasesOxo-Acid-Lyases (vertaling onbekend)Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.D000095D08.586.520.224.600.100Acetolactate SynthaseAcetolactate Synthase (vertaling onbekend)A flavoprotein that catalyzes the formation of acetolactate from 2 moles of pyruvate in the biosynthesis of valine and the formation of acetohydroxybutyrate from pyruvate and alpha-ketobutyrate in the biosynthesis of isoleucine. EC 4.1.3.18.D000878D08.586.520.224.600.200Anthranilate SynthaseAnthranilate Synthase (vertaling onbekend)An enzyme that catalyzes the formation of anthranilate (o-aminobenzoate) and pyruvic acid from chorismate and glutamine. Anthranilate is the biosynthetic precurser of tryptophan and numerous secondary metabolites, including inducible plant defense compounD001275D08.586.520.224.600.300ATP Citrate (pro-S)-LyaseATP Citrate (pro-S)-Lyase (vertaling onbekend)An enzyme that, in the presence of ATP and CoA, catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, ADP, and orthophosphate. This reaction represents an important step in fatty acid biosynthesis. EC 4.1.3.8.D002950D08.586.520.224.600.400Citrate (si)-SynthaseCitrate (si)-Synthase (vertaling onbekend)Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and conenzyme A. EC 4.1.3.7.D006904D08.586.520.224.600.600Hydroxymethylglutaryl-CoA SynthaseHydroxymethylglutaryl-CoA Synthase (vertaling onbekend)An enzyme that catalyzes the synthesis of hydroxymethylglutaryl-CoA from acetyl-CoA and acetoacetyl-CoA. This is a key enzyme in steroid biosynthesis. EC 4.1.3.5.D007522D08.586.520.224.600.700Isocitrate LyaseIsocitrate Lyase (vertaling onbekend)A key enzyme in the glyoxylate cycle. It catalyzes the conversion of isocitrate to succinate and glyoxylate. EC 4.1.3.1.D015079D08.586.520.224.600.8002-Isopropylmalate Synthase2-Isopropylmalate Synthase (vertaling onbekend)An enzyme that catalyzes the first step in the biosynthetic pathway to leucine, forming isopropyl malate from acetyl-CoA and alpha-ketoisovaleric acid. EC 4.1.3.12.D008292D08.586.520.224.600.850Malate SynthaseMalate Synthase (vertaling onbekend)An important enzyme in the glyoxylic acid cycle which reversibly catalyzes the synthesis of L-malate from acetyl-CoA and glyoxylate. EC 4.1.3.2.D014368D08.586.520.224.800TryptophanaseTryptophanase (vertaling onbekend)An enzyme that catalyzes the conversion of L-tryptophan and water to indole, pyruvate, and ammonia. It is a pyridoxal-phosphate protein, requiring K+. It also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan aD014447D08.586.520.224.900Tyrosine Phenol-LyaseTyrosine Phenol-Lyase (vertaling onbekend)An enzyme that catalyzes the cleavage of tyrosine to phenol, pyruvate, and ammonia. It is a pyridoxal phosphate protein. The enzyme also forms pyruvate from D-tyrosine, L-cysteine, S-methyl-L-cysteine, L-serine, and D-serine, although at a slower rate. ECD019759D08.586.520.232Carbon-Nitrogen LyasesCarbon-Nitrogen Lyases (vertaling onbekend)Enzymes that catalyze the cleavage of a carbon-nitrogen bond by means other than hydrolysis or oxidation. Subclasses are the AMMONIA-LYASES, the AMIDINE-LYASES, the amine-lyases, and other carbon-nitrogen lyases. EC 4.3.D019760D08.586.520.232.300Amidine-LyasesAmidine-Lyases (vertaling onbekend)These enzymes catalyze the elimination of ammonia from amidines with the formation of a double bond. EC 4.3.2.D000264D08.586.520.232.300.200Adenylosuccinate LyaseAdenylosuccinate Lyase (vertaling onbekend)An enzyme that, in the course of purine ribonucleotide biosynthesis, catalyzes the conversion of 5'-phosphoribosyl-4-(N-succinocarboxamide)-5-aminoimidazole to 5'-phosphoribosyl-4-carboxamide-5-aminoimidazole and the conversion of adenylosucciniD001123D08.586.520.232.300.400Argininosuccinate LyaseArgininosuccinate Lyase (vertaling onbekend)An enzyme of the urea cycle which splits argininosuccinate to fumarate plus arginine. Its absence leads to the metabolic disease argininosuccinic acidemia in man. EC 4.3.2.1.D000642D08.586.520.232.400Ammonia-LyasesAmmonia-Lyases (vertaling onbekend)Enzymes that catalyze the formation of a carbon-carbon double bond by the elimination of AMMONIA. EC 4.3.1.D001220D08.586.520.232.400.200Aspartate Ammonia-LyaseAspartate Ammonia-Lyase (vertaling onbekend)An enzyme that catalyzes the conversion of aspartic acid to ammonia and fumaric acid in plants and some microorganisms. EC 4.3.1.1.D004981D08.586.520.232.400.350Ethanolamine Ammonia-LyaseEthanolamine Ammonia-Lyase (vertaling onbekend)An enzyme that catalyzes the deamination of ethanolamine to acetaldehyde. EC 4.3.1.7.D006638D08.586.520.232.400.500Histidine Ammonia-LyaseHistidine Ammonia-Lyase (vertaling onbekend)An enzyme that catalyzes the first step of histidine catabolism, forming UROCANIC ACID and AMMONIA from HISTIDINE. Deficiency of this enzyme is associated with elevated levels of serum histidine. EC 4.3.1.3.D011163D08.586.520.232.400.550Hydroxymethylbilane SynthaseHydroxymethylbilane Synthase (vertaling onbekend)An enzyme that catalyzes the formation of hydroxymethylbilane from four molecules of porphobilinogen. EC 4.3.1.8.D010650D08.586.520.232.400.700Phenylalanine Ammonia-LyasePhenylalanine Ammonia-Lyase (vertaling onbekend)An enzyme that catalyzes the deamination of L-phenylalanine to form trans-cinnamate and ammonia. It may also act on L-tyrosine. Since the enzyme deprives neoplastic tissue of phenylalanine, it has been used experimentally in the treatment of acute lymphobD019757D08.586.520.241Carbon-Oxygen LyasesCarbon-Oxygen Lyases (vertaling onbekend)Enzymes that catalyze the cleavage of a carbon-oxygen bond by means other than hydrolysis or oxidation. EC 4.2.D003547D08.586.520.241.150Cysteine SynthaseCysteine Synthase (vertaling onbekend)An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. EC 4.2.99.8.D006836D08.586.520.241.300Hydro-LyasesHydro-Lyases (vertaling onbekend)Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.D000154D08.586.520.241.300.050Aconitate HydrataseAconitate Hydratase (vertaling onbekend)An enzyme that catalyzes the reversible hydration of cis-aconitate to yield citrate or isocitrate. It is one of the citric acid cycle enzymes. EC 4.2.1.3.D002256D08.586.520.241.300.150Carbonic AnhydrasesCarbonic Anhydrases (vertaling onbekend)A family of zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide. They play an important role in the transport of CARBON DIOXIDE from the tissues to the LUNG. EC 4.2.1.1.D024401D08.586.520.241.300.150.100Carbonic Anhydrase ICarbonic Anhydrase I (vertaling onbekend)A cytosolic carbonic anhydrase isoenzyme primarily expressed in ERYTHROCYTES, vascular endothelial cells, and the gastrointestinal mucosa. EC 4.2.1.-D024402D08.586.520.241.300.150.200Carbonic Anhydrase IICarbonic Anhydrase II (vertaling onbekend)A cytosolic carbonic anhydrase isoenzyme found widely distributed in cells of almost all tissues. Deficiencies of carbonic anhydrase II produce a syndrome characterized by OSTEOPETROSIS, renal tubular acidosis (ACIDOSIS, RENAL TUBULAR) and cerebral calcifD024403D08.586.520.241.300.150.300Carbonic Anhydrase IIICarbonic Anhydrase III (vertaling onbekend)A cytosolic carbonic anhydrase isoenzyme primarily expressed in skeletal muscle (MUSCLES, SKELETAL). EC 4.2.1.-D030741D08.586.520.241.300.150.400Carbonic Anhydrase IVCarbonic Anhydrase IV (vertaling onbekend)A membrane-bound carbonic anhydrase found in lung capillaries and kidney.D024404D08.586.520.241.300.150.500Carbonic Anhydrase VCarbonic Anhydrase V (vertaling onbekend)A carbonic anhydrase isoenzyme found in MITOCHONDRIA where it provides bicarbonate ions that are components in the urea cycle and in GLUCONEOGENESIS.D003541D08.586.520.241.300.200Cystathionine beta-SynthaseCystathionine beta-Synthase (vertaling onbekend)A multifunctional pyridoxal phosphate enzyme. In the second stage of cysteine biosynthesis it catalyzes the reaction of homocysteine with serine to form cystathionine with the elimination of water. Deficiency of this enzyme leads to HYPERHOMOCYSTEINEMIA aD004746D08.586.520.241.300.250Enoyl-CoA HydrataseEnoyl-CoA Hydratase (vertaling onbekend)An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of fatty acids and in mitochondrial fatty acid synthesis, has broad specificity, and is most active with crotonD005649D08.586.520.241.300.300Fumarate HydrataseFumarate Hydratase (vertaling onbekend)An enzyme that catalyzes the reversible hydration of fumaric acid to yield L-malic acid. It is one of the citric acid cycle enzymes. EC 4.2.1.2.D010751D08.586.520.241.300.500Phosphopyruvate HydratasePhosphopyruvate Hydratase (vertaling onbekend)An enzyme of the lyase class that catalyzes the dehydration of 2-phosphoglycerate to form phosphoenolpyruvate. (Dorland, 28th ed) EC 4.2.1.11.D000623D08.586.520.241.300.550Porphobilinogen SynthasePorphobilinogen Synthase (vertaling onbekend)An enzyme that catalyzes the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. EC 4.2.1.24.D011302D08.586.520.241.300.600Prephenate DehydratasePrephenate Dehydratase (vertaling onbekend)An enzyme that catalyzes the conversion of prephenate to phenylpyruvate with the elimination of water and carbon dioxide. In the enteric bacteria this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthD011408D08.586.520.241.300.650Propanediol DehydratasePropanediol Dehydratase (vertaling onbekend)An enzyme that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. EC 4.2.1.28.D012695D08.586.520.241.300.750L-Serine DehydrataseL-Serine Dehydratase (vertaling onbekend)An enzyme of the lyase class that catalyzes the dehydration and deamination of L-serine to form pyruvate. (Dorland, 28th ed) EC 4.2.1.13.D013913D08.586.520.241.300.800Threonine DehydrataseThreonine Dehydratase (vertaling onbekend)A pyridoxal-phosphate protein that catalyzes the deamination of threonine to 2-ketobutyrate and ammonia. The role of this enzyme can be biosynthetic or biodegradative. In the former role it supplies 2-ketobutyrate required for isoleucine biosynthesis, whiD014367D08.586.520.241.300.850Tryptophan SynthaseTryptophan Synthase (vertaling onbekend)An enzyme that catalyzes the conversion of L-serine and 1-(indol-3-yl)glycerol 3-phosphate to L-tryptophan and glyceraldehyde 3-phosphate. It is a pyridoxal phosphate protein that also catalyzes the conversion of serine and indole into tryptophan and wateD014559D08.586.520.241.300.900Urocanate HydrataseUrocanate Hydratase (vertaling onbekend)An enzyme that catalyzes the conversion of 4,5-dihydro-4-oxo-5-imidazolepropanoate to urocanate and water. EC 4.2.1.49.D014576D08.586.520.241.300.950Uroporphyrinogen-III SynthaseUroporphyrinogen-III Synthase (vertaling onbekend)An enzyme that catalyzes the cyclization of hydroxymethylbilane to yield uroporphyrinogen III and water. EC 4.2.1.75.D011133D08.586.520.241.700Polysaccharide-LyasesPolysaccharide-Lyases (vertaling onbekend)A group of carbon-oxygen lyases. These enzymes catalyze the breakage of a carbon-oxygen bond in polysaccharides leading to an unsaturated product and the elimination of an alcohol. EC 4.2.2.D002810D08.586.520.241.700.350Chondroitinases and Chondroitin LyasesChondroitinases and Chondroitin Lyases (vertaling onbekend)Enzymes which catalyze the elimination of glucuronate residues from chondroitin A,B, and C or which catalyze the hydrolysis of sulfate groups of the 2-acetamido-2-deoxy-D-galactose 6-sulfate units of chondroitin sulfate. EC 4.2.2.-.D002808D08.586.520.241.700.350.500Chondroitin LyasesChondroitin Lyases (vertaling onbekend)Enzymes which catalyze the elimination of delta-4,5-D-glucuronate residues from polysaccharides containing 1,4-beta-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages thereby bringing about depolymerization. EC 4.2.2.4 acts on chonD019765D08.586.520.241.700.350.500.500Chondroitin ABC LyaseChondroitin ABC Lyase (vertaling onbekend)An enzyme that catalyzes the eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups. (Enzyme NomenclatD019763D08.586.520.241.700.512Heparin LyaseHeparin Lyase (vertaling onbekend)An enzyme of the isomerase class that catalyzes the eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with termD006821D08.586.520.241.700.675HyaluronoglucosaminidaseHyaluronoglucosaminidase (vertaling onbekend)An enzyme that catalyzes the random hydrolysis of 1,4-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate. (From Enzyme Nomenclature, 1992)D013437D08.586.520.300Carbon-Sulfur LyasesCarbon-Sulfur Lyases (vertaling onbekend)Enzymes that catalyze the cleavage of a carbon-sulfur bond by means other than hydrolysis or oxidation. EC 4.4.D003542D08.586.520.300.250Cystathionine gamma-LyaseCystathionine gamma-Lyase (vertaling onbekend)A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyzes the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. EC 4.4.1.1.D007791D08.586.520.300.500Lactoylglutathione LyaseLactoylglutathione Lyase (vertaling onbekend)An enzyme that catalyzes the interconversion of methylglyoxal and lactate, with glutathione serving as a coenzyme. EC 4.4.1.5.D005294D08.586.520.500FerrochelataseFerrochelatase (vertaling onbekend)An enzyme widely distributed in cells and tissues. It is located in the inner mitochondrial membrane and catalyzes the formation of heme from protoporphyrin IX and ferrous ions during the terminal step in the heme biosynthetic pathway. EC 4.99.1.1.D019761D08.586.520.650Phosphorus-Oxygen LyasesPhosphorus-Oxygen Lyases (vertaling onbekend)Enzymes that catalyze the cleavage of a phosphorus-oxygen bond by means other than hydrolysis or oxidation. EC 4.6.D000262D08.586.520.650.200Adenylate CyclaseAdenylate Cyclase (vertaling onbekend)An enzyme of the lyase class that catalyzes the formation of CYCLIC AMP and pyrophosphate from ATP. EC 4.6.1.1.D006162D08.586.520.650.600Guanylate CyclaseGuanylate Cyclase (vertaling onbekend)An enzyme that catalyzes the conversion of GTP to 3',5'-cyclic GMP and pyrophosphate. It also acts on ITP and dGTP. (From Enzyme Nomenclature, 1992) EC 4.6.1.2.D009097D08.586.600Multienzyme ComplexesMultienzyme Complexes (vertaling onbekend)Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates; may involve simply a transfer of water molecules of hydrogen atoms or be associated with large supramolecular structures such as mD000877D08.586.600.075Anthranilate PhosphoribosyltransferaseAnthranilate Phosphoribosyltransferase (vertaling onbekend)An enzyme that catalyzes the formation of N-5'-phosphoribosylanthranilic acid from anthranilate and phosphoribosylpyrophosphate, the first step in tryptophan synthesis in E. coli. It exists in a complex with ANTHRANILATE SYNTHASE in bacteria. EC 2.4.D000878D08.586.600.085Anthranilate SynthaseAnthranilate Synthase (vertaling onbekend)An enzyme that catalyzes the formation of anthranilate (o-aminobenzoate) and pyruvic acid from chorismate and glutamine. Anthranilate is the biosynthetic precurser of tryptophan and numerous secondary metabolites, including inducible plant defense compounD001221D08.586.600.116Aspartate CarbamoyltransferaseAspartate Carbamoyltransferase (vertaling onbekend)An enzyme that catalyzes the conversion of carbamoyl phosphate and L-aspartate to yield orthophosphate and N-carbamoyl-L-aspartate. (From Enzyme Nomenclature, 1992) EC 2.1.3.2.D001225D08.586.600.130Aspartokinase Homoserine DehydrogenaseAspartokinase Homoserine Dehydrogenase (vertaling onbekend)An enzyme complex consisting of aspartokinase, EC 2.7.2.4, and homoserine dehydrogenase, EC 1.1.1.3. The complex has been isolated from E. coli and consists of four identical subunits with a molecular weight of 85,000. The enzyme complex is involved in thD002786D08.586.600.200Cholesterol Monooxygenase (Side-Chain-Cleaving)Cholesterol Monooxygenase (Side-Chain-Cleaving) (vertaling onbekend)Multi-enzyme complex required for the conversion of cholesterol to adrenal cortex hormones. It releases methylpentanoate or isocaproaldehyde and pregnenolone. The complex contains cytochrome P-450, a flavoprotein, a non-heme iron protein, and NADPH. EC 1.D005226D08.586.600.317Fatty Acid Synthetase ComplexFatty Acid Synthetase Complex (vertaling onbekend)blaD007655D08.586.600.465Ketoglutarate Dehydrogenase ComplexKetoglutarate Dehydrogenase Complex (vertaling onbekend)blaD007788D08.586.600.541Lactose SynthaseLactose Synthase (vertaling onbekend)An enzyme of the transferase class that catalyzes the transfer of galactose from UDPgalactose to glucose, forming lactose. The enzyme is a complex of the enzyme N-ACETYLLACTOSAMINE SYNTHASE and alpha-lactalbumin; the latter protein is present in lactatingD010731D08.586.600.700Phosphoenolpyruvate Sugar Phosphotransferase SystemPhosphoenolpyruvate Sugar Phosphotransferase System (vertaling onbekend)The bacterial sugar phosphotransferase system (PTS) that catalyzes the transfer of the phosphoryl group from phosphoenolpyruvate to its sugar substrates (the PTS sugars) concomitant with the translocation of these sugars across the bacterial membrane. TheD011451D08.586.600.720Prostaglandin-Endoperoxide SynthaseProstaglandin-Endoperoxide Synthase (vertaling onbekend)An enzyme complex that catalyzes the formation of prostaglandins from the appropriate unsaturated fatty acid, molecular oxygen, and a reduced acceptor. EC 1.14.99.1.D011768D08.586.600.741Pyruvate Dehydrogenase ComplexPyruvate Dehydrogenase Complex (vertaling onbekend)A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE C (LIPOAMIDE), dihydrolipoamide acetyltransferase and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subjD008058D08.586.600.741.525Lipoamide DehydrogenaseLipoamide Dehydrogenase (vertaling onbekend)A flavoprotein that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of the multienzyme pyruvate dehydrogenase complex and 2-oxoglutarate dehydrogenase complex. EC 1.8.1.4.D030481D08.586.600.741.725Pyruvate Dehydrogenase (Lipoamide)Pyruvate Dehydrogenase (Lipoamide) (vertaling onbekend)The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).D013394D08.586.600.850Sucrase-Isomaltase ComplexSucrase-Isomaltase Complex (vertaling onbekend)An enzyme complex found in the brush border membranes of the small intestine. It is believed to be an enzyme complex with different catalytic sites. Its absence is manifested by an inherited disease called sucrase-isomaltase deficiency.D014367D08.586.600.896Tryptophan SynthaseTryptophan Synthase (vertaling onbekend)An enzyme that catalyzes the conversion of L-serine and 1-(indol-3-yl)glycerol 3-phosphate to L-tryptophan and glyceraldehyde 3-phosphate. It is a pyridoxal phosphate protein that also catalyzes the conversion of serine and indole into tryptophan and wateD014450D08.586.600.925Ubiquinol-Cytochrome-c ReductaseUbiquinol-Cytochrome-c Reductase (vertaling onbekend)An 11-subunit enzyme complex that acts as an electron transferring protein in the mitochondrial respiratory chain. The enzyme complex catalyzes the oxidation of ubiquinol to ubiquinone and ferrocytochrome c in the presence of ferricytochrome c. It containD010088D08.586.682OxidoreductasesOxidoreductases (vertaling onbekend)The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possiD000429D08.586.682.047Alcohol OxidoreductasesAlcohol Oxidoreductases (vertaling onbekend)A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3),D000094D08.586.682.047.050Acetoin DehydrogenaseAcetoin Dehydrogenase (vertaling onbekend)An enzyme that catalyzes the conversion of acetoin to diacetyl in the presence of NAD. EC 1.1.1.5.D000426D08.586.682.047.070Alcohol DehydrogenaseAlcohol Dehydrogenase (vertaling onbekend)A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.D002237D08.586.682.047.150Carbohydrate DehydrogenasesCarbohydrate Dehydrogenases (vertaling onbekend)Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.D005637D08.586.682.047.150.225Fructuronate ReductaseFructuronate Reductase (vertaling onbekend)An enzyme that catalyzes the reversible oxidation of mannonate to fructuronate in the presence of NAD. Also reduces D-tagaturonate to D-altronate. EC 1.1.1.57.D005691D08.586.682.047.150.250Galactose DehydrogenasesGalactose Dehydrogenases (vertaling onbekend)D-Galactose:NAD(P)+ 1-oxidoreductases. Catalyzes the oxidation of D-galactose in the presence of NAD+ or NADP+ to D-galactono-gamma-lactone and NADH or NADPH. Includes EC 1.1.1.48 and EC 1.1.1.120.D005948D08.586.682.047.150.270Glucose DehydrogenasesGlucose Dehydrogenases (vertaling onbekend)D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.D005954D08.586.682.047.150.300Glucosephosphate DehydrogenaseGlucosephosphate Dehydrogenase (vertaling onbekend)blaD010734D08.586.682.047.150.600Phosphogluconate DehydrogenasePhosphogluconate Dehydrogenase (vertaling onbekend)An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27tD013401D08.586.682.047.150.700Sugar Alcohol DehydrogenasesSugar Alcohol Dehydrogenases (vertaling onbekend)Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.D000449D08.586.682.047.150.700.075Aldehyde ReductaseAldehyde Reductase (vertaling onbekend)An enzyme that catalyzes reversibly the oxidation of an aldose to an alditol. It possesses broad specificity for many aldoses. EC 1.1.1.21.D005993D08.586.682.047.150.700.400Glycerolphosphate DehydrogenaseGlycerolphosphate Dehydrogenase (vertaling onbekend)blaD007064D08.586.682.047.150.700.475L-Iditol 2-DehydrogenaseL-Iditol 2-Dehydrogenase (vertaling onbekend)An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14D008354D08.586.682.047.150.700.649Mannitol DehydrogenaseMannitol Dehydrogenase (vertaling onbekend)blaD014533D08.586.682.047.150.900Uridine Diphosphate Glucose DehydrogenaseUridine Diphosphate Glucose Dehydrogenase (vertaling onbekend)An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.D005692D08.586.682.047.210Galactose OxidaseGalactose Oxidase (vertaling onbekend)An enzyme that oxidizes galactose in the presence of molecular oxygen to D-galacto-hexodialdose. It is a copper protein. EC 1.1.3.9.D005949D08.586.682.047.239Glucose OxidaseGlucose Oxidase (vertaling onbekend)An enzyme of the oxidoreductase class that catalyzes the conversion of beta-D-glucose and oxygen to D-glucono-1,5-lactone and peroxide. It is a flavoprotein, highly specific for beta-D-glucose. The enzyme is produced by Penicillium notatum and other fungiD006715D08.586.682.047.370Homoserine DehydrogenaseHomoserine Dehydrogenase (vertaling onbekend)An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.D001225D08.586.682.047.370.060Aspartokinase Homoserine DehydrogenaseAspartokinase Homoserine Dehydrogenase (vertaling onbekend)An enzyme complex consisting of aspartokinase, EC 2.7.2.4, and homoserine dehydrogenase, EC 1.1.1.3. The complex has been isolated from E. coli and consists of four identical subunits with a molecular weight of 85,000. The enzyme complex is involved in thD015094D08.586.682.047.3853-Hydroxyacyl CoA Dehydrogenases3-Hydroxyacyl CoA Dehydrogenases (vertaling onbekend)Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis. EC 1.1.1.35.D006903D08.586.682.047.385.415Hydroxymethylglutaryl CoA ReductasesHydroxymethylglutaryl CoA Reductases (vertaling onbekend)Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A to yield MEVALONIC ACID.D025781D08.586.682.047.385.415.250Hydroxymethylglutaryl-CoA Reductases, NAD-DependentHydroxymethylglutaryl-CoA Reductases, NAD-Dependent (vertaling onbekend)Specific hydroxymethylglutaryl CoA reductases that utilize the cofactor NAD. This class of enzymes performs a catabolic role in microorganisms such as Pseudomonas mevalonii where it oxidatively acetylates MEVALONIC ACID to form 3-HYDROXY-3-METHYLGLUTARYL-D025782D08.586.682.047.385.415.750Hydroxymethylglutaryl-CoA-Reductases, NADP-dependentHydroxymethylglutaryl-CoA-Reductases, NADP-dependent (vertaling onbekend)Specific hydroxymethylglutaryl CoA reductases that utilize the cofactor NAD. In liver enzymes of this class are involved in cholesterol biosynthesis.D006884D08.586.682.047.393Hydroxybutyrate DehydrogenaseHydroxybutyrate Dehydrogenase (vertaling onbekend)blaD006911D08.586.682.047.428Hydroxyprostaglandin DehydrogenasesHydroxyprostaglandin Dehydrogenases (vertaling onbekend)Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.D006913D08.586.682.047.436Hydroxysteroid DehydrogenasesHydroxysteroid Dehydrogenases (vertaling onbekend)Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.D015096D08.586.682.047.436.3503-Hydroxysteroid Dehydrogenases3-Hydroxysteroid Dehydrogenases (vertaling onbekend)Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.D002789D08.586.682.047.436.350.150Cholesterol OxidaseCholesterol Oxidase (vertaling onbekend)An enzyme that catalyzes the oxidation of cholesterol in the presence of molecular oxygen to 4-cholesten-3-one and hydrogen peroxide. The enzyme is not specific for cholesterol, but will also oxidize other 3-hydroxysteroids. EC 1.1.3.6.D011375D08.586.682.047.436.350.700Progesterone ReductaseProgesterone Reductase (vertaling onbekend)An enzyme that catalyzes the reduction of a 3 beta-hydroxy-delta(5)-steroid to 3-oxo-delta(4)-steroid in the presence of NAD. It converts pregnenolone to progesterone and dehydroepiandrosterone to androstenedione. EC 1.1.1.145.D015067D08.586.682.047.436.37517-Hydroxysteroid Dehydrogenases17-Hydroxysteroid Dehydrogenases (vertaling onbekend)A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.D004960D08.586.682.047.436.375.280Estradiol DehydrogenasesEstradiol Dehydrogenases (vertaling onbekend)Enzymes that catalyze the oxidation of estradiol at the 17-hydroxyl group in the presence of NAD+ or NADP+ to yield estrone and NADH or NADPH. The 17-hydroxyl group can be in the alpha- or beta-configuration. EC 1.1.1.62D015089D08.586.682.047.436.40020-Hydroxysteroid Dehydrogenases20-Hydroxysteroid Dehydrogenases (vertaling onbekend)Catalyze the oxidation of 20-hydroxysteroids to 20-ketosteroids. Includes EC 1.1.1.149 and EC 1.1.1.53.D003349D08.586.682.047.436.400.150Cortisone ReductaseCortisone Reductase (vertaling onbekend)An enzyme that catalyzes the interconversion of a ketone and hydroxy group at C-20 of cortisone and other 17,20,21-trihydroxy steroids. EC 1.1.1.53.D007168D08.586.682.047.485IMP DehydrogenaseIMP Dehydrogenase (vertaling onbekend)An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.D007521D08.586.682.047.497Isocitrate DehydrogenaseIsocitrate Dehydrogenase (vertaling onbekend)An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and iD007770D08.586.682.047.547Lactate DehydrogenaseLactate Dehydrogenase (vertaling onbekend)A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of lactate and pyruvate. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.D008291D08.586.682.047.605Malate DehydrogenaseMalate Dehydrogenase (vertaling onbekend)An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.D012264D08.586.682.047.857Ribonucleotide ReductasesRibonucleotide Reductases (vertaling onbekend)blaD012262D08.586.682.047.857.567Ribonucleoside Diphosphate ReductaseRibonucleoside Diphosphate Reductase (vertaling onbekend)An enzyme of the oxidoreductase class that catalyzes the formation of 2'-deoxyribonucleotides from the corresponding ribonucleotides using NADPH as the ultimate electron donor. The deoxyribonucleoside diphosphates are used in DNA synthesis. (From DorD000445D08.586.682.075Aldehyde OxidoreductasesAldehyde Oxidoreductases (vertaling onbekend)blaD000444D08.586.682.075.100Aldehyde DehydrogenaseAldehyde Dehydrogenase (vertaling onbekend)An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. EC 1.2.1.3. Before 1978, it was classified as EC 1.1.1.70.D024601D08.586.682.075.100.500Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) (vertaling onbekend)An NADP-dependent, non-phosphorylating aldehyde dehydrogenase that catalyzes the irreversible oxidation of GLYCERALDEHYDE 3-PHOSPHATE to 3-phosphoglycerate. It is found in the cytosol of a wide variety of organisms.D001223D08.586.682.075.211Aspartate-Semialdehyde DehydrogenaseAspartate-Semialdehyde Dehydrogenase (vertaling onbekend)An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.D005560D08.586.682.075.400Formate DehydrogenasesFormate Dehydrogenases (vertaling onbekend)Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbonD005987D08.586.682.075.532Glyceraldehyde-3-Phosphate DehydrogenasesGlyceraldehyde-3-Phosphate Dehydrogenases (vertaling onbekend)Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that tranD024601D08.586.682.075.532.249Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) (vertaling onbekend)An NADP-dependent, non-phosphorylating aldehyde dehydrogenase that catalyzes the irreversible oxidation of GLYCERALDEHYDE 3-PHOSPHATE to 3-phosphoglycerate. It is found in the cytosol of a wide variety of organisms.D024602D08.586.682.075.532.374Glyceraldehyde 3 Phosphate-Dehydrogenase (NADP+)(Phosphorylating)Glyceraldehyde 3 Phosphate-Dehydrogenase (NADP+)(Phosphorylating) (vertaling onbekend)A phosphorylating glyceraldehyde-3-phosphate dehydrogenase found in the CHLOROPLASTS of higher plants. This enzyme exists as an A2B2 heterotetramer and transfers hydrogen to NADP. It plays an important role in catalyzing the reductive step of the Calvin cD024581D08.586.682.075.532.500Glyceraldehyde-3-Phosphate-Dehydrogenase (Phosphorylating)Glyceraldehyde-3-Phosphate-Dehydrogenase (Phosphorylating) (vertaling onbekend)An NAD-dependent glyceraldehyde-3-phosphate dehydrogenase found in the cytosol of eucaryotes. It catalyses the dehydrogenation and phosphorylation of GLYCERALDEHYDE 3-PHOSPHATE to 3-phospho-D-glyceroyl phosphate, which is an important step in the GLYCOLYSD030481D08.586.682.075.725Pyruvate Dehydrogenase (Lipoamide)Pyruvate Dehydrogenase (Lipoamide) (vertaling onbekend)The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).D000587D08.586.682.107Amine OxidoreductasesAmine Oxidoreductases (vertaling onbekend)Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.D010089D08.586.682.107.582Oxidoreductases, N-DemethylatingOxidoreductases, N-Demethylating (vertaling onbekend)blaD000633D08.586.682.107.582.276Aminopyrine N-DemethylaseAminopyrine N-Demethylase (vertaling onbekend)blaD019392D08.586.682.107.582.338Cytochrome P-450 CYP2E1Cytochrome P-450 CYP2E1 (vertaling onbekend)A polymorphic enzyme that activates carcinogenic N-nitrosamines, benzene, urethane, and other low molecular weight compounds. It is inducible by ethanol and metabilizes alcohol. Experimentally, it is used to study the effects of ethanol usage and withdrawD005037D08.586.682.107.582.400Ethylmorphine-N-DemethylaseEthylmorphine-N-Demethylase (vertaling onbekend)A drug-metabolizing enzyme of the hepatic microsomal oxidase system which catalyzes the oxidation of the N-methyl group of ethylmorphine with the formation of formaldehyde.D011394D08.586.682.107.640Proline OxidaseProline Oxidase (vertaling onbekend)The first enzyme of the proline degradative pathway. It catalyzes the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age. EC 1.D011734D08.586.682.107.680Pyridoxaminephosphate OxidasePyridoxaminephosphate Oxidase (vertaling onbekend)An enzyme catalyzing the deamination of pyridoxaminephosphate to pyridoxal phosphate. It is a flavoprotein that also oxidizes pyridoxine-5-phosphate and pyridoxine. EC 1.4.3.5.D011762D08.586.682.107.695Pyrroline Carboxylate ReductasesPyrroline Carboxylate Reductases (vertaling onbekend)A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD(P)H. Includes both the 2-oxidoreductase (EC 1.5.1.1) and the 5-oxidoreductase (EC 1.5.1.2). The former also reduces 1-piperidine-2-carboxylate to pD012443D08.586.682.107.750Saccharopine DehydrogenasesSaccharopine Dehydrogenases (vertaling onbekend)A collection of enzymes that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-LYSINE or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-GLUTAMATE. Deficiency of this enzyme causes HYPERLYSINEMIAS. EC 1.5.1.D013762D08.586.682.107.825Tetrahydrofolate DehydrogenaseTetrahydrofolate Dehydrogenase (vertaling onbekend)An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monopD000594D08.586.682.135Amino Acid OxidoreductasesAmino Acid Oxidoreductases (vertaling onbekend)A class of enzymes that catalyze oxidation-reduction reactions of amino acids. EC 1.4.-.D006631D08.586.682.135.075Amine Oxidase (Copper-Containing)Amine Oxidase (Copper-Containing) (vertaling onbekend)A group of enzymes including those oxidizing primary monoamines, diamines, and histamine. They are copper proteins, and, as their action depends on a carbonyl group, they are sensitive to inhibition by semicarbazide. EC 1.4.3.6.D003605D08.586.682.135.125D-Amino-Acid OxidaseD-Amino-Acid Oxidase (vertaling onbekend)blaD005969D08.586.682.135.398Glutamate DehydrogenaseGlutamate Dehydrogenase (vertaling onbekend)An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.D018086D08.586.682.135.410Glutamate Dehydrogenase (NADP+)Glutamate Dehydrogenase (NADP+) (vertaling onbekend)An enzyme that catalyzes the conversion of L-glutamate, H2O, and NADP+ to 2-oxoglutarate, NH3, and NADPH. (From Enzyme Nomenclature, 1992) EC 1.4.1.4.D005970D08.586.682.135.470Glutamate SynthaseGlutamate Synthase (vertaling onbekend)An enzyme that catalyzes the formation of 2 molecules of glutamate from glutamine plus alpha-ketoglutarate in the presence of NADPH. EC 1.4.1.13.D008995D08.586.682.135.697Monoamine OxidaseMonoamine Oxidase (vertaling onbekend)An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. It is a flavin-containing enzyme that is localized in mitochondrial membranes, whether in nerve terminals, the liver, or other organs. Monoamine oxidase is important in D001595