| Glutathione hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 MH, Ricketts WA (June 1993). "Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase". Biochemistry. 32 (24): 6302–6. doi: 10.1021/bi00075a026. PMID 8099811.
- ^ Suzuki H, Kumagai H (November 2002). "Autocatalytic processing of gamma-glutamyltranspeptidase". The Journal of Biological Chemistry. 277 (45): 43536–43. doi: 10.1074/jbc.m207680200. PMID 12207027.
- ^ Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K (April 2006). "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. Bibcode: 2006PNAS..103.6471O. doi: 10.1073/pnas.0511020103. PMC 1458908. PMID 16618936.
- ^ Boanca G, Sand A, Okada T, Suzuki H, Kumagai H, Fukuyama K, Barycki JJ (January 2007). "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. doi: 10.1074/jbc.m607694200. PMID 17107958.
- ^ Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K (January 2007). "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. doi: 10.1074/jbc.m607490200. PMID 17135273.
- ^ Wickham S, West MB, Cook PF, Hanigan MH (July 2011). "Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes". Analytical Biochemistry. 414 (2): 208–14. doi: 10.1016/j.ab.2011.03.026. PMC 3099546. PMID 21447318.
- ^ Carter BZ, Wiseman AL, Orkiszewski R, Ballard KD, Ou CN, Lieberman MW (May 1997). "Metabolism of leukotriene C4 in gamma-glutamyl transpeptidase-deficient mice". The Journal of Biological Chemistry. 272 (19): 12305–10. doi: 10.1074/jbc.272.19.12305. PMID 9139674.
External links
- Glutathione+hydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Glutathione hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 MH, Ricketts WA (June 1993). "Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase". Biochemistry. 32 (24): 6302–6. doi: 10.1021/bi00075a026. PMID 8099811.
- ^ Suzuki H, Kumagai H (November 2002). "Autocatalytic processing of gamma-glutamyltranspeptidase". The Journal of Biological Chemistry. 277 (45): 43536–43. doi: 10.1074/jbc.m207680200. PMID 12207027.
- ^ Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K (April 2006). "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. Bibcode: 2006PNAS..103.6471O. doi: 10.1073/pnas.0511020103. PMC 1458908. PMID 16618936.
- ^ Boanca G, Sand A, Okada T, Suzuki H, Kumagai H, Fukuyama K, Barycki JJ (January 2007). "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. doi: 10.1074/jbc.m607694200. PMID 17107958.
- ^ Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K (January 2007). "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. doi: 10.1074/jbc.m607490200. PMID 17135273.
- ^ Wickham S, West MB, Cook PF, Hanigan MH (July 2011). "Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl transpeptidase enzymes". Analytical Biochemistry. 414 (2): 208–14. doi: 10.1016/j.ab.2011.03.026. PMC 3099546. PMID 21447318.
- ^ Carter BZ, Wiseman AL, Orkiszewski R, Ballard KD, Ou CN, Lieberman MW (May 1997). "Metabolism of leukotriene C4 in gamma-glutamyl transpeptidase-deficient mice". The Journal of Biological Chemistry. 272 (19): 12305–10. doi: 10.1074/jbc.272.19.12305. PMID 9139674.
External links
- Glutathione+hydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)