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
- ↑ 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.
- ↑ Suzuki, H.; Kumagai, H. (2002). "Autocatalytic processing of γ-glutamyltranspeptidase". J. Biol. Chem. 277: 43536–43543. doi:10.1074/jbc.m207680200. PMID 12207027.
- ↑ 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. PMID 16618936.
- ↑ 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.
- ↑ 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.
- ↑ 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. PMID 21447318.
- ↑ 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.
External links
- Glutathione hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH)
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