Purification and some properties of L-glycol dehydrogenase from hen's muscle.
1. An enzyme which catalyzes the NAD(P)H-linked reversible reduction of uncharged vicinal dicarbonyls and alpha-hydroxycarbonyls to L-(+)-glycols has been purified from hen's muscle. This enzyme has not been previously described. 2. According to the rules of the I.U.P.A.C.-I.U.B. Enzymes Commission, the systematic name of L-(+)-glycol:NAD(P) oxidoreductase and the trivial name of L-glycol dehydrogenase are proposed for the enzyme. 3. Three forms of this enzyme differing in pI have been isolated; two forms, which together represent about 90% of total recovered activity, and electrophoretically pure. 4. Molecular weight, pH profiles and affinity for substrates are also described.
D000093:Acetoin / Q000378:metabolism; D000429:Alcohol Oxidoreductases / Q000302:isolation & purification*; D000818:Animals; D002072:Butylene Glycols / Q000378:metabolism; D002645:Chickens; D005260:Female; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D009249:NADP / Q000378:metabolism; D013379:Substrate Specificity
D002072:Butylene Glycols; D009249:NADP; D000093:Acetoin; D000429:Alcohol Oxidoreductases; C031043:L-glycol dehydrogenase