Biology:Glutathione hydrolase
From HandWiki
| 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 [math]\displaystyle{ \rightleftharpoons }[/math] L-cysteinylglycine + L-glutamate
This protein also acts as enzyme EC 2.3.2.2 (gamma-glutamyltransferase).
References
- ↑ "Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase". Biochemistry 32 (24): 6302–6. June 1993. doi:10.1021/bi00075a026. PMID 8099811.
- ↑ "Autocatalytic processing of gamma-glutamyltranspeptidase". The Journal of Biological Chemistry 277 (45): 43536–43. November 2002. doi:10.1074/jbc.m207680200. PMID 12207027.
- ↑ "Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate". Proceedings of the National Academy of Sciences of the United States of America 103 (17): 6471–6. April 2006. doi:10.1073/pnas.0511020103. PMID 16618936. Bibcode: 2006PNAS..103.6471O.
- ↑ "Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad". The Journal of Biological Chemistry 282 (1): 534–41. January 2007. doi:10.1074/jbc.m607694200. PMID 17107958.
- ↑ "Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism". The Journal of Biological Chemistry 282 (4): 2433–9. January 2007. doi:10.1074/jbc.m607490200. PMID 17135273.
- ↑ "Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes". Analytical Biochemistry 414 (2): 208–14. July 2011. doi:10.1016/j.ab.2011.03.026. PMID 21447318.
- ↑ "Metabolism of leukotriene C4 in gamma-glutamyl transpeptidase-deficient mice". The Journal of Biological Chemistry 272 (19): 12305–10. May 1997. doi:10.1074/jbc.272.19.12305. PMID 9139674.
External links
- Glutathione+hydrolase at the US National Library of Medicine Medical Subject Headings (MeSH)
 |  |
