Bacterial γ-glutamyltranspeptidases, physiological function, structure, catalytic mechanism and application
Author:
Affiliation:
1. Division of Applied Biology, Kyoto Institute of Technology
2. Department of Biological Sciences, Graduate School of Science, Osaka University
3. Ishikawa Prefectural University
Publisher
Japan Academy
Subject
General Physics and Astronomy,General Agricultural and Biological Sciences,General Medicine
Link
https://www.jstage.jst.go.jp/article/pjab/96/9/96_PJA9609B-05/_pdf
Reference116 articles.
1. 1) Nakayama, R., Kumagai, H. and Tochikura, T. (1984) Purification and properties of γ-glutamyltranspeptidase from Proteus mirabilis. J. Bacteriol. 160, 341–346.
2. 2) Nakayama, R., Kumagai, H. and Tochikura, T. (1982) γ-Glutamylcysteine synthetase from Proteus mirabilis. Agric. Biol. Chem. 46, 1301–1309.
3. 3) Meister, A. and Tate, S.S. (1976) Glutathione and related γ-glutamyl compounds: Biosynthesis and utilization. Annu. Rev. Biochem. 45, 559–604.
4. 4) Meister, A. and Anderson, M.E. (1983) Glutathione. Annu. Rev. Biochem. 52, 711–760.
5. 5) Hasegawa, M. and Matsubara, I. (1978) γ-Glutamylpeptide formative activity of Corynebacterium glutamicum by the reverse reaction of the γ-glutamylpeptides hydrolytic enzyme. Agric. Biol. Chem. 42, 371–381.
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