A mutant Bacillus subtilis γ-glutamyltranspeptidase specialized in hydrolysis activity
A mutant Bacillus subtilis γ-glutamyltranspeptidase specialized in hydrolysis activity
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DOI：
10.1016/s0378-1097(03)00456-7
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发表时间：
2003-07-29
影响因子：
2.1
通讯作者：
Kumagai, H
中科院分区：
文献类型：
--
作者：
Minami, H;Suzuki, H;Kumagai, H
gamma-Glutamyltranspeptidase (GGT) catalyzes the hydrolysis of gamma-glutamyl compounds and the transfer of their gamma-glutamyl moieties to amino acids and peptides. The transpeptidation activity of Bacillus subtilis GGT is about 10-fold higher than its hydrolysis activity. In B. subtilis GGT, substitution of Asp-445 with Ala abolished its transpeptidation activity. The specific activity for hydrolysis of D445A GGT was 40.2% of that of the wild-type GGT. The K-m value for (L)-glutamine was 15.3 mM. D445A GGT was salt tolerant like the wildtype GGT. These results indicate that D445A GGT will be highly useful as a 'glutaminase' in food industry. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
