Molecular cloning and characterization of γ-glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694

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  • IMAOKA Masashi
    Department of Biotechnology, College of Life Sciences, Ritsumeikan University
  • YANO Shigekazu
    Department of Biotechnology, College of Life Sciences, Ritsumeikan University
  • OKUMURA Masashi
    Department of Biotechnology, College of Life Sciences, Ritsumeikan University
  • HIBI Takao
    Department of Bioscience, Faculty of Biotechnology, Fukui Prefectural University
  • WAKAYAMA Mamoru
    Department of Biotechnology, College of Life Sciences, Ritsumeikan University

書誌事項

タイトル別名
  • Molecular Cloning and Characterization of .GAMMA.-Glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694
  • Molecular cloning and characterization of g glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694
  • Molecular Cloning and Characterization of γ-Glutamyltranspeptidase from<i>Pseudomonas nitroreducens</i>IFO12694

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抄録

γ-Glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694 (PnGGT) exhibited higher hydrolytic activity than transfer activity, as compared with other γ-glutamyltranspeptidases (GGTs). PnGGT showed little activity towards most of L-amino acids and towards glycyl-glycine, which is often used as a standard γ-glutamyl accepter in GGT transfer reactions. The preferred substrates for PnGGT as a γ-glutamyl accepter were amines such as methylamine, ethylamine, and isopropylamine.

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