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EC 1.3
This list contains a list of Enzyme Commission number, EC numbers for the first group, EC 1, oxidoreductases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. EC 1.1 Acting on the CH-OH group of donors EC 1.1.1 With Nicotinamide adenine dinucleotide or NADP as acceptor *: alcohol dehydrogenase *: alcohol dehydrogenase (NADP+), alcohol dehydrogenase (NADP+) *: homoserine dehydrogenase *: (R,R)-butanediol dehydrogenase, (''R,R'')-butanediol dehydrogenase * EC 1.1.1.5: acetoin dehydrogenase. Now EC 1.1.1.303, diacetyl reductase [(''R'')-acetoin forming] and EC 1.1.1.304, diacetyl reductase [(''S'')-acetoin forming] *: glycerol dehydrogenase *: propanediol-phosphate dehydrogenase *: glycerol-3-phosphate dehydrogenase (NAD+), glycerol-3-phosphate dehydrogenase (NAD+) *: ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme Commission Number
The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the corresponding enzyme-catalyzed reaction. EC numbers do not specify enzymes but enzyme-catalyzed reactions. If different enzymes (for instance from different organisms) catalyze the same reaction, then they receive the same EC number. Furthermore, through convergent evolution, completely different protein folds can catalyze an identical reaction (these are sometimes called non-homologous isofunctional enzymes) and therefore would be assigned the same EC number. By contrast, UniProt identifiers uniquely specify a protein by its amino acid sequence. Format of number Every enzyme code consists of the letters "EC" followed by four numbers separated by periods. Those numbers represent a progressively finer classification of the enzyme. Preliminary ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Galactitol 2-dehydrogenase
In enzymology, a galactitol 2-dehydrogenase () is an enzyme that catalyzes the chemical reaction :galactitol + NAD+ \rightleftharpoons D-tagatose + NADH + H+ Thus, the two substrates of this enzyme are galactitol and NAD+, whereas its 3 products are D-tagatose, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... of this enzyme class is galactitol:NAD+ 2-oxidoreductase. This enzyme is also called dulcitol dehydrogenase. This enzyme participates in galactose metabolism. References * EC 1.1.1 NADH-dependent enzymes Enzymes of known structure {{1.1.1-enzyme-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glyoxylate Reductase
Glyoxylate reductase (), first isolated from spinach leaves, is an enzyme that catalyzes the reduction of glyoxylate to glycolate, using the cofactor NADH or NADPH. The systematic name of this enzyme class is glycolate:NAD+ oxidoreductase. Other names in common use include NADH-glyoxylate reductase, glyoxylic acid reductase, and NADH-dependent glyoxylate reductase. Structure The crystal structure of the glyoxylate reductase enzyme from the hyperthermophilic archeon Pyrococcus horiskoshii OT3 has been reported. The enzyme exists in the dimeric form. Each monomer has two domains: a substrate-binding domain where glyoxylate binds, and a nucleotide-binding domain where the NAD(P)H cofactor binds. Mechanism The enzyme catalyzes the transfer of a hydride from NAD(P)H to glyoxylate, causing a reduction of the substrate to glycolate and an oxidation of the cofactor to NAD(P)+. Figure 2 shows the mechanism for this reaction. It is thought that the two residues Glu270 and His28 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Shikimate Dehydrogenase
In enzymology, a shikimate dehydrogenase () is an enzyme that catalysis, catalyzes the chemical reaction :shikimate + NADP+ \rightleftharpoons 3-dehydroshikimate + NADPH + H+ Thus, the two substrate (biochemistry), substrates of this enzyme are shikimate and nicotinamide adenine dinucleotide phosphate, NADP+, whereas its 3 product (chemistry), products are 3-dehydroshikimate, nicotinamide adenine dinucleotide phosphate, NADPH, and hydrogen ion, H+. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis. Function Shikimate dehydrogenase is an enzyme that catalyzes one step of the shikimic acid, shikimate pathway. This pathway is found in bacteria, plants, fungi, algae, and parasites and is responsible for the biosynthesis of aromatic amino acids (phenylalanine, tyrosine, and tryptophan) from the metabolism of carbohydrates. In contrast, animals and humans lack this pathway hence products of this biosynthetic route are essential amino acids that must be ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Quinate Dehydrogenase
In enzymology, a quinate dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-quinate + NAD+ \rightleftharpoons 3-dehydroquinate + NADH + H+ Thus, the two substrates of this enzyme are L-quinate and NAD+, whereas its 3 products are 3-dehydroquinate, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... of this enzyme class is L-quinate:NAD+ 3-oxidoreductase. Other names in common use include quinic dehydrogenase, quinate:NAD oxidoreductase, quinate 5-dehydrogenase, and quinate:NAD+ 5-oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis. Reference ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Histidinol Dehydrogenase
In enzymology, histidinol dehydrogenase (HIS4) (HDH) () is an enzyme that catalyzes the chemical reaction : L-histidinol + 2 NAD+ \rightleftharpoons L-histidine + 2 NADH + 2 H+ Thus, the two substrates of this enzyme are L-histidinol and NAD+, whereas its 3 products are L-histidine, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-histidinol:NAD+ oxidoreductase. This enzyme is also called L-histidinol dehydrogenase. Structure In bacteria, HDH is a single chain polypeptide; in fungi it is the C-terminal domain of a multifunctional enzyme which catalyses three different steps of histidine biosynthesis; and in plants it is expressed as a nuclear encoded protein precursor which is exported to the chloroplast. Active site Histidinol is held inside the active site thanks to a zinc ion, but the zinc ion does not part ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
(R)-4-hydroxyphenyllactate Dehydrogenase
(R)-4-hydroxyphenyllactate dehydrogenase () is an enzyme that catalyzes a chemical reaction :(R)-3-(4-hydroxyphenyl)lactate + NAD(P)+ \rightleftharpoons 3-(4-hydroxyphenyl)pyruvate + NAD(P)H + H The 3 substrates of this enzyme are (R)-3-(4-hydroxyphenyl)lactate, NAD, and NADP, whereas its 4 products are 3-(4-hydroxyphenyl)pyruvate, NADH, NADPH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name of this enzyme class is (R)-3-(4-hydroxyphenyl)lactate:NAD(P) 2-oxidoreductase. Other names in common use include (R)-aromatic lactate dehydrogenase, and D-hydrogenase, D-aryllactate. This enzyme participates in tyrosine and phenylalanine Phenylalanine (symbol Phe or F) is an essential α-amino acid with the chemical formula, formula . It can be viewed as a benzyl group substituent, substituted for the methyl group of alanine, or a phenyl group in place of a terminal hy ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
UDP-glucose 6-dehydrogenase
UDP-glucose 6-dehydrogenase is a cytosolic enzyme that in humans is encoded by the ''UGDH'' gene. The protein encoded by this gene converts UDP-glucose to UDP-glucuronate and thereby participates in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosylated compounds are common components of the extracellular matrix and likely play roles in signal transduction, cell migration, and cancer growth and metastasis. The expression of this gene is up-regulated by transforming growth factor beta and down-regulated by hypoxia. This enzyme participates in 4 metabolic pathways: pentose and glucuronate interconversions, ascorbate and aldarate metabolism, starch and sucrose metabolism, and nucleotide sugars metabolism. Loss of UGDH has recently been implicated in epileptic encephalopathy in humansHengel, H., Bosso-Lefèvre, C., Grady, G. et al. Loss-of-function mutations in UDP-Glucose 6-Dehydrogenase cause recessive developmen ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aldose Reductase
In enzymology, aldose reductase (or aldehyde reductase) () is an enzyme in humans encoded by the gene AKR1B1. It is an cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides, and primarily known for catalyzing the reduction of glucose to sorbitol, the first step in polyol pathway of glucose metabolism. Reactions Aldose reductase catalyzes the NADPH-dependent conversion of glucose to sorbitol, the first step in polyol pathway of glucose metabolism. The second and last step in the pathway is catalyzed by sorbitol dehydrogenase, which catalyzes the NAD-linked oxidation of sorbitol to fructose. Thus, the polyol pathway results in conversion of glucose to fructose with stoichiometric utilization of NADPH and production of NADH. ;glucose + NADPH + H+ \rightleftharpoons sorbitol + NADP+ Galactose is also a substrate for the polyol pathway, but the corresponding keto sugar is not produced because sorbito ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
(+)-neomenthol Dehydrogenase
In enzymology, a (+)-neomenthol dehydrogenase () is an enzyme that catalyzes the chemical reaction :(+)-neomenthol + NADP \rightleftharpoons (−)-menthone + NADPH + H Thus, the two substrates of this enzyme are (+)-neomenthol and NADP, whereas its 3 products are (−)-menthone, NADPH, and H. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD or NADP as acceptor. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... of this enzyme class is (+)-neomenthol:NADP oxidoreductase. This enzyme is also called monoterpenoid dehydrogenase. This enzyme participates in monoterpenoid biosynthesis. References * EC 1.1.1 NADPH-dependent enzymes Enzymes of unknown structure {{1.1.1-enzyme-s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glucuronolactone Reductase
In enzymology, a glucuronolactone reductase () is an enzyme that catalyzes the chemical reaction :L-gulono-1,4-lactone + NADP+ \rightleftharpoons D-glucurono-3,6-lactone + NADPH + H+ Thus, the two substrates of this enzyme are L-gulono-1,4-lactone and NADP+, whereas its 3 products are D-glucurono-3,6-lactone, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name A systematic name is a name given in a systematic way to one unique group, organism, object or chemical substance, out of a specific population or collection. Systematic names are usually part of a nomenclature. A semisystematic name or semitrivi ... of this enzyme class is L-gulono-1,4-lactone:NADP+ 1-oxidoreductase. Other names in common use include GRase, and gulonolactone dehydrogenase. This enzyme participates in ascorbate and aldarate metabolism. References * EC 1.1.1 NADPH-depe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
