GGT dimers hydrolyse GSH

Stable Identifier
R-HSA-8943279
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
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
18357469 The human gamma-glutamyltransferase gene family

Heisterkamp, N, Groffen, J, Warburton, D, Sneddon, TP

Hum Genet 2008
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, Guellaƫn, 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
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
glutathione hydrolase activity of GGT dimers [plasma membrane]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
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