Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.
Detected in fetal and adult kidney and liver, adult pancreas, stomach, intestine, placenta and lung. Isoform 3 is lung-specific. There are several other tissue-specific forms that arise from alternative promoter usage but that produce the same protein.
Sulfur metabolism; glutathione metabolism.
Involvement in disease
Defects in GGT1 are a cause of glutathionuria (GLUTH) [MIM:231950]; also known as gamma-glutamyltranspeptidase deficiency. It is an autosomal recessive disease.
Belongs to the gamma-glutamyltransferase family.
N-glycosylated on both chains. Contains hexoses, hexosamines and sialic acid residues. Glycosylation profiles tested in kidney and liver tissues reveal the presence of tissue-specific and site-specific glycan composition, despite the overlap in composition among the N-glycans. A total of 36 glycan compositions, with 40 unique structures are observed. Up to 15 different glycans are observed at a single site, with site-specific variation in glycan composition. The difference in glycosylation profiles in the 2 tissues do not affect the enzyme activity.
Baumann T et al. Glutathione-conjugated sulfanylalkanols are substrates for ABCC11 and ?-glutamyl transferase 1: a potential new pathway for the formation of odorant precursors in the apocrine sweat gland. Exp Dermatol23:247-52 (2014).
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