| 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... |
| 11 beta-HSD | 11 Beta-hydroxysteroid dehydrogenase |
|---|---|
| 11 beta-OHSD | 11 beta-Hydroxysteroid dehydrogenase |
| 11 beta-HSD-1 | 11 beta-Hydroxysteroid dehydrogenase type 1 |
| 11 beta-HSD2 | 11 beta-Hydroxysteroid dehydrogenase type 2 |
| 15-PGDH | 15-Hydroxy-prostaglandin dehydrogenase |
| saccharopine dehydrogenase | Two enzymes that are used in the pathway of l-lysine catabolism; the first isoform catalyses the reversible conversion of l-lysine, alpha-ketoglutarate, and NADH to saccharopine and NAD+; the other isoform reversibly catalyses to conversion of saccharopine and NAD+ to l-glutamate, NADH, and l-alpha-aminoadipate d-saemialdehyde. A deficiency of one of these isoforms is associated with familial hyperlysinaemia and saccharopinuria. (05 Mar 2000) |
|---|---|
| saccharopine dehydrogenases | <enzyme> N-5-(1,3-dicarboxypropyl)-l-lysine:NAD(p)+ oxidoreductase (l-lysine-forming). Catalyses the oxidative cleavage of saccharopine to lysine plus ketoglutaric acid. Requires NAD; EC 1.5.1.8 requires NADP. Registry number: EC 1.5.1. (12 Dec 1998) |
| saccharopine | HOOC(CH2)2CH(COOH)NH(CH2)4CH(NH2)COOH;a derivative of alpha-ketoglutarate and l-lysine that is an intermediate in l-lysine catabolism; elevated in cases of saccharopinuria. (05 Mar 2000) |
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| saccharopine oxidase | <enzyme> Flavoenzyme which catalyses the oxidative cleavage of saccharopine to delta-1-piper9deine-6-carboxylate, glutamate and h2o2 Registry number: EC 1.5.3.- (26 Jun 1999) |
| 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) |
| aldehyde dehydrogenase | <enzyme> An enzyme that oxidises an aldehyde in the presence of NAD+ and water to an acid and NADH. Before 1978, it was classified as EC 1.1.1.70. Chemical name: Aldehyde:NAD+ oxidoreductase Registry number: EC 1.2.1.3 (12 Dec 1998) |
| aldehyde dehydrogenase (acylating) | An oxidoreductase converting an aldehyde and CoA to acyl-CoA with NAD+ as H acceptor. (05 Mar 2000) |
| aldehyde dehydrogenase (NAD+) | An oxidoreductase reversibly converting aldehydes to acids with NADP+ as H acceptor. (05 Mar 2000) |
Synonyms : Lysine-2-Oxoglutarate Reductase, Lysine-Ketoglutarate Reductase, Saccharopine Dehydrogenase (NAD+, L-Glutamate Forming), Saccharopine Dehydrogenase (NAD+, L-Lysine Forming), Saccharopine Dehydrogenase (NADP+, L-Glutamate Forming)
| saccharopine dehydrogenase (NAD+, L-glutamate-forming) |
[EC 1.5.1.9] an enzyme activity that catalyzes oxidative cleavage of saccharopine to form α-aminoadipate semialdehyde and glutamate, using NAD+ as an electron acceptor. The reaction is the second step in the major route of lysine degradation; the enzyme activity is part of the bifunctional enzyme α-aminoadipic semialdehyde synthase (q.v.). The enzyme activity is absent in hyperlysinemia and the variant saccharopinuria.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
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| saccharopine dehydrogenase (NADP+, L-lysine-forming) |
[EC 1.5.1.8] an enzyme activity that catalyzes the condensation of L-lysine and α-ketoglutarate to form saccharopine, using NADPH as an electron donor. The reaction is the initial step in the major route of lysine degradation; the enzyme activity is part of the bifunctional enzyme α-aminoadipic semialdehyde synthase (q.v.). The enzyme activity is absent in hyperlysinemia and substantially reduced in the variant saccharopinuria. Usually called lysine ketoglutarate reductase.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
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