Gamma-glutamyltranspeptidase, conserved site
IPR055262
Definition
This entry represents a conserved site of GGTs. Gamma-glutamyltranspeptidase ([ec:2.3.2.2]) (GGT) PMID:2868390 catalyses 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. This entry also includes the highly similar Scoloptoxin SSD14 from Scolopendra dehaani. SSD14 (which is also cleaved into alpha and beta subunits) has been shown to induce human platelet aggregation PMID:23148443. 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.
7 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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