Glutamine-induced production and secretion of Helicobacter pylori gamma-glutamyltranspeptidase at low pH and its putative role in glutathione transport.

Department of Biotechnology and Bioinformatics, College of Science and Technology, Korea University, Sejong 339-700, Korea.

Journal of microbiology and biotechnology 2013 Apr

filter terms:

Helicobacter pylori increased the gamma-glutamyltranspeptidase (GGT) production under low-pH (maximal at pH 4) and appropriate pCO2 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 (~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. pylori, but not by the one pretreated with a potent GGT inhibitor, acivicin, suggesting that the GGT may partake in glutathione uptake by the cell.

Citation

Mi Ran Ki, Na Rae Yun, Se Young Hwang. Glutamine-induced production and secretion of Helicobacter pylori gamma-glutamyltranspeptidase at low pH and its putative role in glutathione transport. Journal of microbiology and biotechnology. 2013 Apr;23(4):467-72