Purification and characterization of alpha-keto amide reductase from Saccharomyces cerevisiae |
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| Authors: | Ishihara Kohji Yamamoto Hiroaki Mitsuhashi Kazuya Nishikawa Kazuyoshi Tsuboi Sadao Tsuji Hideaki Nakajima Nobuyoshi |
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| Institution: | Department of Life Science, Okayama University of Science, Okayama, Japan. ishihara@das.ous.ac.jp |
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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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