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gamma-glutamyltransferase-1 (GGT1, gamma-glutamyltranspeptidase-1, CD224 antigen)

Function: - initiates extracellular glutathione (GSH) breakdown - provides cells with a local cysteine supply - contributes to maintain intracelular GSH level - part of cell antioxidant defense mechanism - catalyzes transfer of glutamyl moiety of glutathione to amino acids & dipeptide acceptors - alternatively, glutathione can be hydrolyzed to give cys-gly & gamma glutamate (reversible) - isoform 3 seems to be inactive - sulfur metabolism; glutathione metabolism (5-L-glutamyl)-peptide + an amino acid peptide + 5-L-glutamyl amino acid Structure: - heterodimer composed of the light & heavy chains - the active site is located in the light chain - belongs to the gamma-glutamyltransferase family - contains hexoses, hexosamines & sialic acid residues - not known if the sialic acid residues are present on N-linked glycans or on O-linked glycans - N-glycosylated on both chains Compartment: membrane Alternative splicing: - named isoforms=3 - alternative promoter usage Expression: - detected in fetal & adult kidney & liver, adult pancreas, stomach, intestine, placenta & lung - isoform 3 is lung-specific - several other tissue-specific forms that arise from alternative promoter usage but that produce the same protein Pathology: - defects in GGT1 are a cause of glutathionuria Note: - Cys-454 was thought to bind the gamma-glutamyl moiety, but mutagenesis of this residue had no effect on activity

General

cluster-of-differentiation antigen; cluster designation antigen; CD antigen gamma-glutamyltransferase (GGT) or gamma-glutamyltranspeptidase glycoprotein

Properties

SIZE: entity length = 569 aa MW = 61 kD COMPARTMENT: cellular membrane MOTIF: transmembrane domain {5-26} N-glycosylation site {N95} N-glycosylation site {N120} N-glycosylation site {N230} N-glycosylation site {N266} N-glycosylation site {N297} N-glycosylation site {N344} N-glycosylation site {N511}

Database Correlations

OMIM 231950 UniProt P19440 Pfam PF01019 KEGG correlations ENZYME 2.3.2.2

References

  1. UniProt :accession P19440
  2. Wikipedia, gamma-glutamyl transpeptidase entry http://en.wikipedia.org/wiki/gamma_glutamyl_transpeptidase