Glutathione hydrolase 1 proenzyme

Definition:

Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as leukotriene C4, LTC4). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4.; [Isoform 3]: Seems to be inactive.

References:

[1]. L A Wetmore, et al. Human lung expresses unique gamma-glutamyl transpeptidase transcripts. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7461-5. [Content Brief]

[2]. Y Ikeda, et al. Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase. J Biol Chem. 1995 Sep 22;270(38):22223-8. [Content Brief]

[3]. Y Ikeda, et al. Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J Biochem. 1996 Jun;119(6):1166-70. [Content Brief]

[4]. Stephanie Wickham, et al. Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes. Anal Biochem. 2011 Jul 15;414(2):208-14. [Content Brief]

[5]. Jesmond Dalli, et al. Maresin conjugates in tissue regeneration biosynthesis enzymes in human macrophages. Proc Natl Acad Sci U S A. 2016 Oct 25;113(43):12232-12237. [Content Brief]

[6]. Matthew B West, et al. Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue. J Biol Chem. 2010 Sep 17;285(38):29511-24. [Content Brief]

[7]. Matthew B West, et al. Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme. J Biol Chem. 2013 Nov 1;288(44):31902-13. [Content Brief]

[8]. Y Ikeda, et al. Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit. J Biol Chem. 1995 May 26;270(21):12471-5. [Content Brief]

[9]. Y Ikeda, et al. Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis. J Biol Chem. 1993 Feb 25;268(6):3980-5. [Content Brief]

[10]. Roselyne Castonguay, et al. Kinetic characterization and identification of the acylation and glycosylation sites of recombinant human gamma-glutamyltranspeptidase. Biochemistry. 2007 Oct 30;46(43):12253-62. [Content Brief]

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