| GDH | glucose dehydrogenase; glutamate dehydrogenase; glycerophosphate dehydrogenase; glycol dehydrogenase... |
|---|---|
| GPD | glucose-6-phosphate dehydrogenase; glycerol-phosphate dehydrogenase |
| LAD | lactic acid dehydrogenase; left anterior descending [artery]; left axis deviation; leukocyte adhesio... |
| LADH | lactic acid dehydrogenase; liver alcohol dehydrogenase |
| PDH | past dental history; phosphate dehydrogenase; position-of-the-dynamometer-handle [test]; progressive... |
| OHHL | N-(3-oxohexanoyl)-L-homoserine lactone |
|---|---|
| AHL | N-Acyl homoserine lactone |
| 11 beta-HSD | 11 Beta-hydroxysteroid dehydrogenase |
| 11 beta-OHSD | 11 beta-Hydroxysteroid dehydrogenase |
| 11 beta-HSD-1 | 11 beta-Hydroxysteroid dehydrogenase type 1 |
| homoserine dehydrogenase | <enzyme> An enzyme that catalyses the reduction of aspartic beta-saemialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. Chemical name: L-Homoserine:NAD(P)+ oxidoreductase Registry number: EC 1.1.1.3 (12 Dec 1998) |
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| aspartokinase homoserine dehydrogenase | An enzyme complex consisting of aspartokinase, and homoserine dehydrogenase, 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 the biosynthesis of amino acids of the aspartate family. (12 Dec 1998) |
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| homoserine | An amino acid which is used by plants and bacteria to make methionine, threonine, and isoleucine (three of the twenty amino acids used to make proteins). Homoserine is similar to the amino acid serine (another of the twenty amino acids used to make proteins), except it has an extra methylene group. It is also formed when cystathionine is metabolised into the amino acid cysteine (another of the twenty amino acids used to make proteins). (09 Oct 1997) |
| homoserine deaminase | <enzyme> A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyses the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. Chemical name: L-Cystathionine cysteine-lyase (deaminating) Registry number: EC 4.4.1.1 (12 Dec 1998) |
| homoserine dehydratase | <enzyme> A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyses the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. Chemical name: L-Cystathionine cysteine-lyase (deaminating) Registry number: EC 4.4.1.1 (12 Dec 1998) |
| homoserine lactone | The cyclic ester (i.e., the d-lactone) of homoserine; formed by the reaction of cyanogen bromide on methionyl residues in peptides and proteins. (05 Mar 2000) |
| acetaldehyde dehydrogenase | <enzyme> Works with both nad and nadp Registry number: EC 1.2.1.5 Synonym: aldehyde dehydrogenase (NADP+), naho gene product (26 Jun 1999) |
| acetoin dehydrogenase | <enzyme> An enzyme that catalyses the conversion of acetoin to diacetyl in the presence of NAD. Chemical name: Acetoin:NAD+ oxidoreductase Registry number: EC 1.1.1.5 (12 Dec 1998) |
| acetol dehydrogenase | <enzyme> Forms methylglyoxal; uses nad+ Registry number: EC 1.1.1.- Synonym: 1-hydroxyacetone dehydrogenase (26 Jun 1999) |
| acyl-ACP dehydrogenase | enoyl-ACP reductase (NADPH) |
| acyl-CoA dehydrogenase | <enzyme> See also records for specific fatty acyl groups which have full EC nomenclature number; electron-transferring flavoprotein system reducing ubiquinone and other acceptors; formerly EC 1.3.2.2 Registry number: EC 1.3.99.3 Synonym: fatty-acyl CoA dehydrogenase, palmitoyl-CoA dehydrogenase, short-chain acyl-CoA dehydrogenase, acyl-coenzyme a dehydrogenase, lauroyl-CoA oxidase (26 Jun 1999) |
| acyl-CoA dehydrogenase (NADPH+) | Enzyme catalyzing the reversible reduction of enoyl-CoA derivatives of chain length 4 to 16, with NADPH as the hydrogen donor, forming acyl-CoA and NADP+. Synonym: enoyl-CoA reductase. (05 Mar 2000) |
| alanopine dehydrogenase | <enzyme> Catalyses reductive elimination between pyruvate and alanine, or glycine, utilizing NADH as coenzyme, producing 2,2'-iminodipropionic acid (alanopine) Registry number: EC 1.5.1.- (26 Jun 1999) |
| alcohol dehydrogenase | <enzyme> An enzyme that catalyses reversibly the final step of alcoholic fermentation by reducing an aldehyde to an alcohol. In the case of ethanol, acetaldehyde is reduced to ethanol in the presence of NADH and hydrogen. The enzyme is a zinc protein which acts on primary and secondary alcohols or hemiacetals. Chemical name: Alcohol:NAD+ oxidoreductase Registry number: EC 1.1.1.1 (12 Dec 1998) |
| alcohol dehydrogenase (acceptor) | An oxidoreductase that reversibly converts primary alcohols to aldehydes with an H acceptor other than NADP+. (05 Mar 2000) |
| alcohol dehydrogenase (NADP+) | An oxidoreductase reversibly converting alcohols to aldehydes (or ketones) with NAD(P)+ as H acceptor. Synonym: aldehyde reductase, DPNH aldehyde transhydrogenase. (05 Mar 2000) |
Synonyms : Dehydrogenase, Homoserine
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