来自还原硝基假单胞菌IFO12694的γ-谷氨酰转肽酶的分子克隆与特性分析
Molecular cloning and characterization of γ-glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694.
作者信息
Imaoka Masashi, Yano Shigekazu, Okumura Masashi, Hibi Takao, Wakayama Mamoru
机构信息
Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Shiga, Japan.
出版信息
Biosci Biotechnol Biochem. 2010;74(9):1936-9. doi: 10.1271/bbb.100199. Epub 2010 Sep 7.
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.
与其他γ-谷氨酰转肽酶（GGT）相比，来自还原硝基假单胞菌IFO12694的γ-谷氨酰转肽酶（PnGGT）表现出更高的水解活性而非转移活性。PnGGT对大多数L-氨基酸以及对甘氨酰甘氨酸几乎没有活性，而甘氨酰甘氨酸在GGT转移反应中常被用作标准γ-谷氨酰受体。PnGGT作为γ-谷氨酰受体的首选底物是胺类，如甲胺、乙胺和异丙胺。
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