Molecular Cloning and Characterization of [gamma]-Glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694

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...

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Published inBioscience, biotechnology, and biochemistry Vol. 74; no. 9; p. 1936
Main Authors IMAOKA, Masashi, YANO, Shigekazu, OKUMURA, Masashi, HIBI, Takao, WAKAYAMA, Mamoru
Format Journal Article
LanguageEnglish
Published Tokyo Oxford University Press 01.09.2010
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Summary: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.
ISSN:0916-8451
1347-6947