Abstract
Escherichia coli K-12 can utilize a gamma-glutamyl peptide as an amino acid source, for which gamma-glutamyltranspeptidase (EC 2.3.2.2) is essential. We suggest that the gamma-glutamyl linkage of a gamma-glutamyl peptide is hydrolyzed by gamma-glutamyltranspeptidase located in the periplasmic space, and the released amino acid is taken up and utilized by E. coli.
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Selected References
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- Camakaris H., Pittard J. Regulation of tyrosine and phenylalanine biosynthesis in Escherichia coli K-12: properties of the tyrR gene product. J Bacteriol. 1973 Sep;115(3):1135–1144. doi: 10.1128/jb.115.3.1135-1144.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Carter T. H., Miller C. G. Aspartate-specific peptidases in Salmonella typhimurium: mutants deficient in peptidase E. J Bacteriol. 1984 Aug;159(2):453–459. doi: 10.1128/jb.159.2.453-459.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cho E. S., Johnson N., Snider B. C. Tissue glutathione as a cyst(e)ine reservoir during cystine depletion in growing rats. J Nutr. 1984 Oct;114(10):1853–1862. doi: 10.1093/jn/114.10.1853. [DOI] [PubMed] [Google Scholar]
- Higashi T., Tateishi N., Naruse A., Sakamoto Y. A novel physiological role of liver glutathione as a reservoir of L-cysteine. J Biochem. 1977 Jul;82(1):117–124. doi: 10.1093/oxfordjournals.jbchem.a131659. [DOI] [PubMed] [Google Scholar]
- Jackson E. N., Yanofsky C. Internal deletions in the tryptophan operon of Escherichia coli. J Mol Biol. 1972 Nov 14;71(2):149–161. doi: 10.1016/0022-2836(72)90343-9. [DOI] [PubMed] [Google Scholar]
- Meister A., Anderson M. E. Glutathione. Annu Rev Biochem. 1983;52:711–760. doi: 10.1146/annurev.bi.52.070183.003431. [DOI] [PubMed] [Google Scholar]
- Miller C. G., Mackinnon K. Peptidase mutants of Salmonella typhimurium. J Bacteriol. 1974 Oct;120(1):355–363. doi: 10.1128/jb.120.1.355-363.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Miller C. G., Schwartz G. Peptidase-deficient mutants of Escherichia coli. J Bacteriol. 1978 Aug;135(2):603–611. doi: 10.1128/jb.135.2.603-611.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Suzuki H., Kumagai H., Echigo T., Tochikura T. DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt. J Bacteriol. 1989 Sep;171(9):5169–5172. doi: 10.1128/jb.171.9.5169-5172.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Suzuki H., Kumagai H., Echigo T., Tochikura T. Molecular cloning of Escherichia coli K-12 ggt and rapid isolation of gamma-glutamyltranspeptidase. Biochem Biophys Res Commun. 1988 Jan 15;150(1):33–38. doi: 10.1016/0006-291x(88)90482-2. [DOI] [PubMed] [Google Scholar]
- Suzuki H., Kumagai H., Tochikura T. Isolation, genetic mapping, and characterization of Escherichia coli K-12 mutants lacking gamma-glutamyltranspeptidase. J Bacteriol. 1987 Sep;169(9):3926–3931. doi: 10.1128/jb.169.9.3926-3931.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Suzuki H., Kumagai H., Tochikura T. gamma-Glutamyltranspeptidase from Escherichia coli K-12: formation and localization. J Bacteriol. 1986 Dec;168(3):1332–1335. doi: 10.1128/jb.168.3.1332-1335.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Suzuki H., Kumagai H., Tochikura T. gamma-Glutamyltranspeptidase from Escherichia coli K-12: purification and properties. J Bacteriol. 1986 Dec;168(3):1325–1331. doi: 10.1128/jb.168.3.1325-1331.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tate S. S., Meister A. gamma-Glutamyl transpeptidase: catalytic, structural and functional aspects. Mol Cell Biochem. 1981 Sep 25;39:357–368. doi: 10.1007/BF00232585. [DOI] [PubMed] [Google Scholar]
- Yen C., Green L., Miller C. G. Degradation of intracellular protein in Salmonella typhimurium peptidase mutants. J Mol Biol. 1980 Oct 15;143(1):21–33. doi: 10.1016/0022-2836(80)90122-9. [DOI] [PubMed] [Google Scholar]
- Yen C., Green L., Miller C. G. Peptide accumulation during growth of peptidase deficient mutants. J Mol Biol. 1980 Oct 15;143(1):35–48. doi: 10.1016/0022-2836(80)90123-0. [DOI] [PubMed] [Google Scholar]