Family

Gamma-glutamyltranspeptidase (IPR000101)

Short name: GGT_peptidase

Family relationships

None.

Description

Gamma-glutamyltranspeptidase (EC:2.3.2.2) (GGT) [PMID: 2868390] catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification [PMID: 1378736]. In prokaryotes and eukaryotes, it is an enzyme that consists of two polypeptide chains, a heavy and a light subunit, processed from a single chain precursor by an autocatalytic cleavage. The active site of GGT is known to be located in the light subunit. The sequences of mammalian and bacterial GGT show a number of regions of high similarity [PMID: 2570061]. Pseudomonas cephalosporin acylases (EC:3.5.1) that convert 7-beta-(4-carboxybutanamido)-cephalosporanic acid (GL-7ACA) into 7-aminocephalosporanic acid (7ACA) and glutaric acid are evolutionary related to GGT and also show some GGT activity [PMID: 1358202]. Like GGT, these GL-7ACA acylases, are also composed of two subunits.

As an autocatalytic peptidase GGT belongs to MEROPS peptidase family T3 (gamma-glutamyltransferase family, clan PB(T)). The active site residue for members of this family and family T1 is C-terminal to the autolytic cleavage site. The type example is gamma-glutamyltransferase 1 from Escherichia coli.

GO terms

Biological Process

GO:0006751 glutathione catabolic process

Molecular Function

GO:0036374 glutathione hydrolase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam
PANTHER
PANTHER
PROSITE patterns
PRINTS
TIGRFAMs