Reactome | GGT dimers hydrolyse GSH

GGT dimers hydrolyse GSH

Stable Identifier

R-HSA-8943279

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane, extracellular region

ReviewStatus

5/5

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GGT (gamma-glutamyl transpeptidase) dimers associated with the plasma membrane (Hanigan & Frierson 1996) hydrolyze extracellular glutathione (GSH) to form cysteinylglycine (CysGly) and glutamate (L-Glu). GGT1 has been extensively characterized. The active dimeric form of the enzyme is generated by autohydrolysis (West et al. 2011) and in vitro can catalyze both the reaction of GSH with water annotated here, and the reaction of GSH with a free amino acid or dipeptide to generate a gamma-glutamyl-amino acid and cysteinylglycine (Castonguay et al. 2007; Pawlak et al. 1989; Tate & Ross 1977; Thompson & Meister 1976). Based on amino acid sequence similarity, Heisterkamp et al. (2008) identified five additional dimeric proteins, GGT2, 3P, 5, 6, and 7, likely to catalyze the same reactions. West et al. (2013), however, found that GGT2 had no catalytic activity in vitro.

Literature References

PubMed ID	Title	Journal	Year
18357469	The human gamma-glutamyltransferase gene family Heisterkamp, N, Groffen, J, Warburton, D, Sneddon, TP	Hum Genet	2008
17924658	Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidase Castonguay, R, Halim, D, Morin, M, Furtos, A, Lherbet, C, Bonneil, E, Thibault, P, Keillor, JW	Biochemistry	2007
9080	Hydrolysis and transfer reactions catalyzed by gamma-glutamyl transpeptidase; evidence for separate substrate sites and for high affinity of L-cystine Thompson, GA, Meister, A	Biochem. Biophys. Res. Commun.	1976
8813074	Immunohistochemical detection of gamma-glutamyl transpeptidase in normal human tissue Hanigan, MH, Frierson, HF	J. Histochem. Cytochem.	1996
23682772	Human GGT2 does not autocleave into a functional enzyme: A cautionary tale for interpretation of microarray data on redox signaling West, MB, Wickham, S, Parks, EE, Sherry, DM, Hanigan, MH	Antioxid. Redox Signal.	2013
21712391	Autocatalytic cleavage of human gamma-glutamyl transpeptidase is highly dependent on N-glycosylation at asparagine 95 West, MB, Wickham, S, Quinalty, LM, Pavlovicz, RE, Li, C, Hanigan, MH	J. Biol. Chem.	2011
2573352	Different gamma-glutamyl transpeptidase mRNAs are expressed in human liver and kidney Pawlak, A, Wu, SJ, Bulle, F, Suzuki, A, Chikhi, N, Ferry, N, Baik, JH, Siegrist, S, Guellaën, G	Biochem Biophys Res Commun	1989
19463	Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit Tate, SS, Ross, ME	J Biol Chem	1977