| PDH | past dental history; phosphate dehydrogenase; position-of-the-dynamometer-handle [test]; progressive... |
|---|---|
| PGD | phosphogluconate dehydrogenase; phosphoglyceraldehyde dehydrogenase; prostaglandin D |
| SDH | serine dehydratase; sorbitol dehydrogenase; spinal dorsal horn; subdural hematoma; succinate dehydro... |
| ACh | Acetyl-Choline |
| DPCC | Di-Palmitoyl Phosphatidyl Choline |
| choline-phosphate cytidylyltransferase | <enzyme> An enzyme that catalyses the transfer of cytidylate (CMP) to choline phosphate to form CDPcholine. It is the rate-limiting enzyme in the choline pathway for the biosynthesis of phosphatidylcholine. Its activity is increased by glucocorticoids. Registry number: EC 2.7.7.15 (12 Dec 1998) |
|---|---|
| choline phosphokinase | <enzyme> An enzyme that is active in the first step of choline phosphoglyceride (lecithin) biosynthesis by catalyzing the phosphorylation of choline to phosphorylcholine in the presence of ATP. Ethanolamine and its methyl and ethyl derivatives can also act as acceptors. Chemical name: ATP:choline phosphotransferase Registry number: EC 2.7.1.32 (12 Dec 1998) |
| choline salicylate | Choline salt of salicyclic acid, an analgesic and antipyretic (because of the salicylate moiety). (05 Mar 2000) |
| choline theophyllinate | A true salt of theophylline; it has mild diuretic, myocardial stimulating vasodilator, and bronchodilator actions, with the same uses as theophylline, but is better absorbed and less irritating. Synonym: choline theophyllinate. (05 Mar 2000) |
| cytidine diphosphate choline | <chemical> Donor of choline in biosynthesis of choline-containing phosphoglycerides. Pharmacological action: nootropic agents. Chemical name: Cytidine 5'-(trihydrogen diphosphate), P'-(2-(trimethylammonio)ethyl) ester, inner salt (12 Dec 1998) |
| 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) |