174.53.163.119 at 04:03, 29 April 2013

2013-04-29T04:03:57Z

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{{Infobox enzyme
| Name = Glutathione hydrolase
| EC_number = 3.4.19.13
| CAS_number =
| IUBMB_EC_number = 3/4/19/13
| GO_code =
| image =
| width =
| caption =
}}
'''Glutathione hydrolase''' ({{EC number|3.4.19.13}}, ''glutathionase'', ''GGT'', ''gamma-glutamyltranspeptidase'') is an [[enzyme]].<ref>{{cite journal | title = Extracellular glutathione is a source of cysteine for cells that express γ-glutamyl transpeptidase |author = Hanigan, M.H. and Ricketts, W.A. |journal = Biochemistry |year = 1993 |volume = 32 |pages = 6302–6306 |pmid = 8099811}}</ref><ref>{{cite journal | title = Autocatalytic processing of γ-glutamyltranspeptidase |author = Suzuki, H. and Kumagai, H. |journal = J. Biol. Chem. |year = 2002 |volume = 277 |pages = 43536–43543 |pmid = 12207027}}</ref><ref>{{cite journal | title = Crystal structures of γ-glutamyltranspeptidase from ''Escherichia coli'', a key enzyme in glutathione metabolism, and its reaction intermediate |author = Okada, T., Suzuki, H., Wada, K., Kumagai, H. and Fukuyama, K. |journal = Proc. Natl. Acad. Sci. USA |year = 2006 |volume = 103 |pages = 6471–6476 |pmid = 16618936}}</ref><ref>{{cite journal | title = Autoprocessing of ''Helicobacter pylori'' γ-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad |author = Boanca, G., Sand, A., Okada, T., Suzuki, H., Kumagai, H., Fukuyama, K. and Barycki, J.J. |journal = J. Biol. Chem. |year = 2007 |volume = 282 |pages = 534–541 |pmid = 17107958}}</ref><ref>{{cite journal | title = Crystal structure of the γ-glutamyltranspeptidase precursor protein from ''Escherichia coli''. Structural changes upon autocatalytic processing and implications for the maturation mechanism |author = Okada, T., Suzuki, H., Wada, K., Kumagai, H. and Fukuyama, K. |journal = J. Biol. Chem. |year = 2007 |volume = 282 |pages = 2433–2439 |pmid = 17135273}}</ref><ref>{{cite journal | title = Gamma-glutamyl compounds: substrate specificity of γ-glutamyl transpeptidase enzymes |author = Wickham, S., West, M.B., Cook, P.F. and Hanigan, M.H. |journal = Anal. Biochem. |year = 2011 |volume = 414 |pages = 208–214 |pmid = 21447318}}</ref><ref>{{cite journal | title = Metabolism of leukotriene C<sub>4</sub> in γ-glutamyl transpeptidase-deficient mice |author = Carter, B.Z., Wiseman, A.L., Orkiszewski, R., Ballard, K.D., Ou, C.N. and Lieberman, M.W. |journal = J. Biol. Chem. |year = 1997 |volume = 272 |pages = 12305–12310 |pmid = 9139674}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

: [[glutathione]] + H<sub>2</sub>O <math>\rightleftharpoons</math> L-cysteinylglycine + L-[[glutamate]]

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

== References ==
{{reflist}}

== External links ==
* {{MeshName|Glutathione+hydrolase}}

[[Category:EC 3.4.19]]

Nu function - Revision history

174.53.163.119 at 04:03, 29 April 2013