Purification and Characterization of α-Keto Amide Reductase from Saccharomyces cerevisiae

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Author(s)

Abstract

An NADPH-dependent α-keto amide reductase was purified from <I>Saccharomyces cerevisiae</I>. 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 α-keto amides but also for aliphatic and aromatic α-keto esters. The internal sequence of the enzyme was identical with that of a hypothetical protein (ORF YDL 124w) coded by yeast chromosome IV.

Journal

  • Bioscience, Biotechnology, and Biochemistry

    Bioscience, Biotechnology, and Biochemistry 68(11), 2306-2312, 2004-11-23

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

References:  21

Codes

  • NII Article ID (NAID)
    130000030919
  • NII NACSIS-CAT ID (NCID)
    AA10824164
  • Text Lang
    ENG
  • Article Type
    ART
  • ISSN
    09168451
  • NDL Article ID
    7173544
  • NDL Source Classification
    ZR7(科学技術--農林水産--農産) // ZR2(科学技術--生物学--生化学) // ZP1(科学技術--化学・化学工業)
  • NDL Call No.
    Z53-G223
  • Data Source
    CJP  NDL  J-STAGE 
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