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Purification and characterization of alpha-keto amide reductase from Saccharomyces cerevisiae.

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

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.

Biosci. Biotechnol. Biochem. 68:2306-2312(2004) [PubMed] [Europe PMC]

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