Molecular Cloning and Characterization of γ-Glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694
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概要
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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.
- 社団法人 日本農芸化学会の論文
著者
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YANO Shigekazu
Department of Biotechnology, Faculty of Life Sciences, Ritsumeikan University
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WAKAYAMA Mamoru
Department of Biotechnology, Faculty of Life Sciences, Ritsumeikan University
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HIBI Takao
Department of Bioscience, Fukui Prefectural University
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IMAOKA Masashi
Department of Biotechnology, College of Life Sciences, Ritsumeikan University
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OKUMURA Masashi
Department of Biotechnology, College of Life Sciences, Ritsumeikan University
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