Reference: Ishihara K, et al. (2004) Purification and characterization of alpha-keto amide reductase from Saccharomyces cerevisiae. Biosci Biotechnol Biochem 68(11):2306-12

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Abstract


An NADPH-dependent alpha-keto amide reductase was purified from Saccharomyces cerevisiae. The molecular mass of the native enzyme was estimated to be 33 and 36 kDa by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis, respectively. The purified enzyme showed a reducing activity not only for aromatic alpha-keto amides but also for aliphatic and aromatic alpha-keto esters. The internal sequence of the enzyme was identical with that of a hypothetical protein (ORF YDL 124w) coded by yeast chromosome IV.

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Journal Article
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Ishihara K, Yamamoto H, Mitsuhashi K, Nishikawa K, Tsuboi S, Tsuji H, Nakajima N
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