Purification, characterization and some properties of diacetyl(acetoin) reductase from Enterobacter aerogenes.
A new method, faster, milder and more efficient than the one previously described [Bryn, K., Hetland, O. & Stormer, F. C. (1971) Eur. J. Biochem, 18, 116-119], for purification of diacetyl(acetoin) reductase from Enterobacter aerogenes is proposed. The experiments carried out with the electrophoretically pure preparations obtained by this procedure show that the enzyme (a) produces L-glycols from the corresponding L-alpha-hydroxycarbonyls by reversible reduction of their oxo groups and also reduces the oxo group of uncharged alpha-dicarbonyls converting them into L-alpha-hydroxycarbonyls, and (b) is specific for NAD. This is a new enzyme for which we suggest the systematic name of L-glycol: NAD+ oxidoreductase and the recommended name of L-glycol dehydrogenase(NAD). The molecular mass, pI, affinity for substrates and pH profiles of this enzyme are also described.
Carballo
J
J
Laboratory of Food Technology and Biochemistry, Facultad de Veterinaria, Universidad de León, Spain.
Martin
R
R
Bernardo
A
A
Gonzalez
J
J
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity / Q000379:methods; D002848:Chromatography, DEAE-Cellulose / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D004754:Enterobacter / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D013237:Stereoisomerism; D013379:Substrate Specificity
D000429:Alcohol Oxidoreductases; C019801:butanediol dehydrogenase