Helicobacter pylori gamma-glutamyl transpeptidase (H. pylori GGT)

Helicobacter pylori gamma-glutamyl transpeptidase is a bacterial enzyme, classified as an N-terminal nucleophile (Ntn) hydrolase, essential for Helicobacter pylori colonization and virulence in the human stomach[1][4][5]. This enzyme catalyzes the hydrolysis and transpeptidation of γ-glutamyl bonds in substrates such as glutathione and glutamine, producing glutamate and ammonia, which can help neutralize gastric acid and modulate the host environment for bacterial survival[1][4][5]. H. pylori GGT is produced as a proenzyme and autocatalytically cleaved to form an active heterodimer with a large and small subunit, with the active site located in the small subunit[1][4][5]. The enzyme acts both extracellularly (secreted or periplasmic form) and plays a role in immune evasion, nutrient acquisition, and possibly gastric pathology associated with H. pylori infection[1][5]. Inhibition of H. pylori GGT is an experimental anti-virulence strategy under consideration for therapeutic development.

Other names

H. pylori GGTγ-glutamyl transpeptidase (bacterial)Gamma-glutamyltranspeptidase

Enzyme inhibitors (e.g., acivicin) block γ-glutamyl bond hydrolysis, inhibiting GGT's catalytic function[3] Potential immunomodulation, as GGT affects glutathione metabolism and ammonia production