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
Search PMC articles PubMed articles NCBI proteins

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 $\rightleftharpoons$ L-cysteinylglycine + L-glutamate

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

References

1. Hanigan, M.H. and 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. and 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. and 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.
4. Boanca, G., Sand, A., Okada, T., Suzuki, H., Kumagai, H., Fukuyama, K. and 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. and 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. and 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.
7. Carter, B.Z., Wiseman, A.L., Orkiszewski, R., Ballard, K.D., Ou, C.N. and 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)