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Published on: July 15, 2011
Occurrence of gamma-glutamyl transpeptidase activity in several mycobacteria including Mycobacterium leprae
Abstract:
gamma-Glutamyl transpeptidase (gamma-GT) activity, which catalyzes the transfer of the "gamma-glutamyl" group of gamma-glutamyl compounds to several dipeptide and amino acid acceptors, was found to be present in several mycobacteria, including M. leprae, both in cell suspensions and in cell-free sonicates. Glycyl D-amino acids were active as acceptors, particularly glycyl-D-alanine and alpha, epsilon-diaminopimelic acid, among the amino acids. Two mycobacterial isolates obtained from biopsy material of lepromatous patients also exhibited similar enzyme activity. The need for further work to delineate the possible role of gamma-GT in mycobacterial metabolism is strongly indicated.
Insights
gamma-Glutamyl transpeptidase (gamma-GT) enzyme activity was detected in mycobacteria, including M. leprae. This finding suggests a potential role for gamma-GT in mycobacterial metabolism, warranting further investigation.
Area of Science:
- Biochemistry
- Microbiology
- Enzymology
Background:
- gamma-Glutamyl transpeptidase (gamma-GT) is an enzyme involved in amino acid metabolism.
- Mycobacteria are a genus of bacteria that includes important human pathogens like Mycobacterium tuberculosis and Mycobacterium leprae.
- The presence and role of gamma-GT in mycobacteria have not been extensively studied.
Purpose of the Study:
- To investigate the presence and activity of gamma-glutamyl transpeptidase (gamma-GT) in various mycobacteria.
- To identify potential substrates and acceptors for the gamma-GT enzyme in mycobacterial systems.
- To explore the implications of gamma-GT activity for mycobacterial metabolism.
Main Methods:
- Enzyme assays were performed on cell suspensions and cell-free sonicates of mycobacteria.
- Various dipeptides and amino acids were tested as potential acceptors for the gamma-glutamyl group.
- Mycobacterial isolates from lepromatous patient biopsies were analyzed for gamma-GT activity.
Main Results:
- gamma-Glutamyl transpeptidase (gamma-GT) activity was confirmed in several mycobacteria, including M. leprae.
- Glycyl D-amino acids, specifically glycyl-D-alanine, and alpha, epsilon-diaminopimelic acid demonstrated significant acceptor activity.
- Similar enzyme activity was observed in two mycobacterial isolates from lepromatous leprosy patients.
Conclusions:
- The study confirms the presence of gamma-glutamyl transpeptidase (gamma-GT) activity in mycobacteria.
- The identified substrates suggest a role for gamma-GT in amino acid metabolism within these bacteria.
- Further research is essential to fully elucidate the metabolic significance of gamma-GT in mycobacteria.

