title: Purification and characterization of an anti-Prelog alcohol dehydrogenase from Oenococcus oeni that reduces 2-octanone to (R)-2-octanol.
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.
authors.affiliation: Key Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, 214122 Wuxi, Jiangsu, China.
authors.forename: Fantao
authors.initials: F
authors.lastname: Meng
authors.forename: Yan
authors.initials: Y
authors.lastname: Xu
mesh_terms: D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007659:Ketones / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008670:Metals / Q000378:metabolism; D008970:Molecular Weight; D009249:NADP / Q000378:metabolism; D000442:Octanols / Q000737:chemistry / Q000378:metabolism*; D056585:Oenococcus / Q000201:enzymology*; D010084:Oxidation-Reduction; D013237:Stereoisomerism; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D007659:Ketones; D008670:Metals; D000442:Octanols; D009249:NADP; C067943:2-octanol; D000426:Alcohol Dehydrogenase; C037075:2-octanone