Biology:Glutathione gamma-glutamylcysteinyltransferase
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glutathione gamma-glutamylcysteinyltransferase | |||||||||
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Identifiers | |||||||||
EC number | 2.3.2.15 | ||||||||
CAS number | 125390-02-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a glutathione gamma-glutamylcysteinyltransferase (EC 2.3.2.15) is an enzyme that catalyzes the chemical reaction
- glutathione + [Glu(-Cys)]n-Gly [math]\displaystyle{ \rightleftharpoons }[/math] Gly + [Glu(-Cys)]n+1-Gly
Thus, the two substrates of this enzyme are glutathione and [Glu(-Cys)]n-Gly, whereas its two products are Gly and [Glu(-Cys)]n+1-Gly.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is glutathione:poly(4-glutamyl-cysteinyl)glycine 4-glutamylcysteinyltransferase. Other names in common use include phytochelatin synthase, and gamma-glutamylcysteine dipeptidyl transpeptidase.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2BTW and 2BU3.
References
- "Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)". Proc. Natl. Acad. Sci. USA 86 (18): 6838–6842. 1989. doi:10.1073/pnas.86.18.6838. PMID 16594069. Bibcode: 1989PNAS...86.6838G.
Original source: https://en.wikipedia.org/wiki/Glutathione gamma-glutamylcysteinyltransferase.
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