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摘要
gamma-Glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694 (PnGGT) exhibited higher hydrolytic activity than transfer activity, as compared with other gamma-glutamyltranspeptidases (GGTs). PnGGT showed little activity towards most of L-amino acids and towards glycyl-glycine, which is often used as a standard gamma-glutamyl accepter in GGT transfer reactions. The preferred substrates for PnGGT as a gamma-glutamyl accepter were amines such as methylamine, ethylamine, and isopropylamine.
- 出版日期2010-9
