Occurrence of gamma-glutamyl transpeptidase activity in several mycobacteria including Mycobacterium leprae.
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.
D000818:Animals; D006801:Humans; D009161:Mycobacterium / Q000201:enzymology*; D009166:Mycobacterium leprae / Q000201:enzymology*; D009168:Mycobacterium phlei / Q000201:enzymology; D051381:Rats; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
D005723:gamma-Glutamyltransferase