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Glutamine-Induced Production and Secretion of Helicobacter pylori gamma-Glutamyltranspeptidase at Low pH and Its Putative Role in Glutathione Transport

Authors
Ki, Mi RamYun, Na RaeHwang, Se Young
Issue Date
4월-2013
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
Keywords
Helicobacter pylori; gamma-glutamyltranspeptidase; glutamine; glutathione; ammonia
Citation
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.23, no.4, pp.467 - 472
Indexed
SCIE
SCOPUS
KCI
Journal Title
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume
23
Number
4
Start Page
467
End Page
472
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/103640
DOI
10.4014/jmb.1210.10035
ISSN
1017-7825
Abstract
Helicobacter pylon increased the gamma-glutamyltranspeptidase (GGT) production under low-pH (maximal at pH 4) and appropriate pCO(2) conditions, while the production of GGT mRNA correlated with increased total enzyme activity. At pH 4, the bacterium augmented enzyme production in the presence of glutamine (similar to 10 mM) in the medium, which predominantly occurred after a 6-min time-lag. Monovalent salts such as NaCl or NH4Cl facilitated enzymatic activation in acidic solutions of approximately pH 4.5. In addition, glutathione's gamma-glutamyl moiety cysteinylglycine appeared to be taken up readily by the intact H. pylon, but not by the one pretreated with a potent GGT inhibitor, acivicin, suggesting that the GGT may partake in glutathione uptake by the cell.
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