Purification and preliminary characterization of alcohol dehydrogenase from Aspergillus nidulans.
Aspergillus alcohol dehydrogenase is produced in response to growth in the presence of a wide variety of inducers, of which the most effective are short-chain alcohols and ketones, e.g. butan-2-one and propan-2-ol. The enzyme can be readily extracted from fresh or freeze-dried cells and purified to homogeneity on Blue Sepharose in a single step by using specific elution with NAD+ and pyrazole. The pure enzyme has Mr 290 000 by electrophoresis or gel filtration; it is a homopolymer with subunit Mr 37 500 by electrophoresis in sodium dodecyl sulphate; its amino acid composition corresponds to Mr 37 900, and the native enzyme contains one zinc atom per subunit. The enzyme is NAD-specific and has a wide substrate activity in the forward and reverse reactions; its activity profile is not identical with those of other alcohol dehydrogenases.
Creaser
E H
EH
Porter
R L
RL
Britt
K A
KA
Pateman
J A
JA
Doy
C H
CH
D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D001233:Aspergillus nidulans / Q000201:enzymology*; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction / Q000187:drug effects; D007700:Kinetics; D013379:Substrate Specificity
D000596:Amino Acids; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase