| Literature DB >> 15564669 |
Kohji Ishihara1, Hiroaki Yamamoto, Kazuya Mitsuhashi, Kazuyoshi Nishikawa, Sadao Tsuboi, Hideaki Tsuji, Nobuyoshi Nakajima.
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.Entities:
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Year: 2004 PMID: 15564669 DOI: 10.1271/bbb.68.2306
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043