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
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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  ⇌ {\displaystyle \rightleftharpoons } L-cysteinylglycine + L-glutamate

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

## References

[edit]

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.

## External links

[edit]

* Glutathione+hydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

* v
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Hydrolase: proteases (EC 3.4)

3.4.11-19: Exopeptidase|

| 3.4.11|

* Aminopeptidase
* Alanine
* Arginyl
* Aspartyl
* Cystinyl
* Leucyl
* Glutamyl
* Methionyl
* 1
* 2
* O

|

3.4.13|

* Dipeptidase
* 1
* 2
* 3

3.4.14|

* Dipeptidyl peptidase
* Cathepsin C
* Dipeptidyl peptidase-4
* Tripeptidyl peptidase
* Tripeptidyl peptidase I
* Tripeptidyl peptidase II

3.4.15|

* Angiotensin-converting enzyme

3.4.16|

* Serine type carboxypeptidases: Cathepsin A
* DD-transpeptidase

3.4.17|

Metalloexopeptidases
Carboxypeptidase

Glutamate II

Other/ungrouped|

* Metalloexopeptidase

3.4.21-25: Endopeptidase|

* Serine protease
* Cysteine protease
* Aspartic acid protease
* Metalloendopeptidase
* Threonine endopeptidase
* Proteasome endopeptidase complex
* HslU—HslV peptidase

* Other/ungrouped: Amyloid precursor protein secretase
* Alpha secretase
* Beta-secretase 1
* Beta-secretase 2
* Gamma secretase

3.4.99: Unknown|

* Staphylokinase

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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)

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* Biology

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