Glutathione hydrolase

Glutathione hydrolase
Identifiers
EC number 3.4.19.13
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Glutathione hydrolase (EC 3.4.19.13, glutathionase, GGT, gamma-glutamyltranspeptidase) is an enzyme.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction

glutathione + H2O L-cysteinylglycine + L-glutamate

This protein also acts as enzyme EC 2.3.2.2 (gamma-glutamyltransferase).

References

  1. ↑ Hanigan, M.H.; Ricketts, W.A. (1993). "Extracellular glutathione is a source of cysteine for cells that express γ-glutamyl transpeptidase". Biochemistry. 32: 6302–6306. doi:10.1021/bi00075a026. PMID 8099811.
  2. ↑ Suzuki, H.; Kumagai, H. (2002). "Autocatalytic processing of γ-glutamyltranspeptidase". J. Biol. Chem. 277: 43536–43543. doi:10.1074/jbc.m207680200. PMID 12207027.
  3. ↑ Okada, T.; Suzuki, H.; Wada, K.; Kumagai, H.; Fukuyama, K. (2006). "Crystal structures of γ-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate". Proc. Natl. Acad. Sci. USA. 103: 6471–6476. doi:10.1073/pnas.0511020103. PMC 1458908. PMID 16618936.
  4. ↑ Boanca, G.; Sand, A.; Okada, T.; Suzuki, H.; Kumagai, H.; Fukuyama, K.; Barycki, J.J. (2007). "Autoprocessing of Helicobacter pylori γ-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad". J. Biol. Chem. 282: 534–541. doi:10.1074/jbc.m607694200. PMID 17107958.
  5. ↑ Okada, T.; Suzuki, H.; Wada, K.; Kumagai, H.; Fukuyama, K. (2007). "Crystal structure of the γ-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism". J. Biol. Chem. 282: 2433–2439. doi:10.1074/jbc.m607490200. PMID 17135273.
  6. ↑ Wickham, S.; West, M.B.; Cook, P.F.; Hanigan, M.H. (2011). "Gamma-glutamyl compounds: substrate specificity of γ-glutamyl transpeptidase enzymes". Anal. Biochem. 414: 208–214. doi:10.1016/j.ab.2011.03.026. PMC 3099546. PMID 21447318.
  7. ↑ Carter, B.Z.; Wiseman, A.L.; Orkiszewski, R.; Ballard, K.D.; Ou, C.N.; Lieberman, M.W. (1997). "Metabolism of leukotriene C4 in γ-glutamyl transpeptidase-deficient mice". J. Biol. Chem. 272: 12305–12310. doi:10.1074/jbc.272.19.12305. PMID 9139674.
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