PROSITE documentation PDOC00404
Gamma-glutamyltranspeptidase signature


γ-glutamyltranspeptidase (EC (GGT) [1] catalyzes the transfer of the γ-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 γ-glutamyl cycle, a pathway for the synthesis and degradation of glutathione. 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. 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 [2]. Pseudomonas cephalosporin acylases (EC 3.5.1.-) that convert 7-β-(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 [3]. Like GGT, these GL-7ACA acylases, are also composed of two subunits.

One of the conserved regions correspond to the N-terminal extremity of the mature light chains of these enzymes. We have used this region as a signature pattern.

Last update:

November 1997 / Pattern and text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

G_GLU_TRANSPEPTIDASE, PS00462; Gamma-glutamyltranspeptidase signature  (PATTERN)


1AuthorsTate S.S. Meister A.
TitleGamma-glutamyl transpeptidase from kidney.
SourceMethods Enzymol. 113:400-419(1985).
PubMed ID2868390

2AuthorsSuzuki H. Kumagai H. Echigo T. Tochikura T.
TitleDNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt.
SourceJ. Bacteriol. 171:5169-5172(1989).
PubMed ID2570061

3AuthorsIshiye M. Niwa M.
TitleNucleotide sequence and expression in Escherichia coli of the cephalosporin acylase gene of a Pseudomonas strain.
SourceBiochim. Biophys. Acta 1132:233-239(1992).
PubMed ID1358202

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