Abstract
An anti-Prelog alcohol dehydrogenase from Oenococcus oeni that reduces 2-octanone to (R)-2-octanol was purified by 26-fold to homogeneity. The enzyme had a homodimeric structure consisting of 49 kDa subunits, required NADPH, but not NADH, as a cofactor and was a Zn-independent short-chain dehydrogenase. Aliphatic methyl ketones (chain length > or =6 carbon atoms) and aromatic methyl ketones were the preferred substrates for the enzyme, the best being 2-octanone. Maximum enzyme activity with 2-octanone was at 45 degrees C and at pH 8.0.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alcohol Dehydrogenase / chemistry
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Alcohol Dehydrogenase / isolation & purification
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Alcohol Dehydrogenase / metabolism*
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Bacterial Proteins / chemistry
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism*
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Hydrogen-Ion Concentration
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Ketones / chemistry
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Ketones / metabolism*
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Kinetics
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Metals / metabolism
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Molecular Weight
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NADP / metabolism
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Octanols / chemistry
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Octanols / metabolism*
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Oenococcus / enzymology*
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Oxidation-Reduction
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Stereoisomerism
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Substrate Specificity
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Temperature
Substances
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Bacterial Proteins
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Ketones
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Metals
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Octanols
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NADP
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2-octanol
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Alcohol Dehydrogenase
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2-octanone