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Template:STRUCTURE 4gg2

Contents 1 The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1 2 Disease 3 Function 4 About this Structure 5 Reference

The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1

Template:ABSTRACT PUBMED 24047895

Disease

[GGT1_HUMAN] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.

Function

[GGT1_HUMAN] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular 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.^{[1] [2]}

About this Structure

4gg2 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA.

Reference

• West MB, Chen Y, Wickham S, Heroux A, Cahill K, Hanigan MH, Mooers BH. Novel insights into eukaryotic gamma-glutamyl transpeptidase 1 from the crystal structure of the glutamate-bound human enzyme. J Biol Chem. 2013 Sep 18. PMID:24047895 doi:http://dx.doi.org/10.1074/jbc.M113.498139

1. ↑ Wetmore LA, Gerard C, Drazen JM. Human lung expresses unique gamma-glutamyl transpeptidase transcripts. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7461-5. PMID:7689219
2. ↑ West MB, Segu ZM, Feasley CL, Kang P, Klouckova I, Li C, Novotny MV, West CM, Mechref Y, Hanigan MH. Analysis of site-specific glycosylation of renal and hepatic gamma-glutamyl transpeptidase from normal human tissue. J Biol Chem. 2010 Sep 17;285(38):29511-24. doi: 10.1074/jbc.M110.145938. Epub, 2010 Jul 9. PMID:20622017 doi:10.1074/jbc.M110.145938