Purification and Characterization of an NADH-Dependent Alcohol Dehydrogenase from Candida maris for the Synthesis of Optically Active 1-(Pyridyl)ethanol Derivatives
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概要
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A novel (R)-specific alcohol dehydrogenase (AFPDH) produced by Candida maris IFO10003 was purified to homogeneity by ammonium sulfate fractionation, DEAE-Toyopearl, and Phenyl-Toyopearl, and characterized. The relative molecular mass of the native enzyme was found to be 59,900 by gel filtration, and that of the subunit was estimated to be 28,900 on SDS-polyacrylamide gel electrophoresis. These results suggest that the enzyme is a homodimer. It required NADH as a cofactor and reduced various kinds of carbonyl compounds, including ketones and aldehydes. AFPDH reduced acetylpyridine derivatives, β-keto esters, and some ketone compounds with high enantioselectivity. This is the first report of an NADH-dependent, highly enantioselective (R)-specific alcohol dehydrogenase isolated from a yeast. AFPDH is a very useful enzyme for the preparation of various kinds of chiral alcohols.
- 社団法人 日本農芸化学会の論文
著者
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Kawano Shigeru
Frontier Biochemical And Medicinal Res. Laboratories Kaneka Corp.
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YANO Miho
Frontier Biochemical and Medicinal Research Laboratories, Kaneka Corporation
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HASEGAWA Junzo
Frontier Biochemical and Medicinal Research Laboratories, Kaneka Corporation
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YASOHARA Yoshihiko
Frontier Biochemical and Medicinal Research Laboratories, Kaneka Corporation
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Yano Miho
Frontier Biochemical And Medicinal Res. Laboratories Kaneka Corp.
関連論文
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