Glutathione hydrolase

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Glutathione hydrolase
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
PMC
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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

^ 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)

[1] 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.

[2] 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.

[3] 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.

[4] 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.

[5] 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.

[6] 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.

[7] 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.

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)