In enzymology, a glutathione gamma-glutamylcysteinyltransferase (EC 2.3.2.15) is an enzyme that catalyzes the chemical reaction
| glutathione gamma-glutamylcysteinyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.2.15 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
- glutathione + [Glu(-Cys)]n-Gly 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
editAs of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2BTW and 2BU3.
References
edit- Grill E, Loffler S, Winnacker E-L, Zenk MH (1989). "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. Bibcode:1989PNAS...86.6838G. doi:10.1073/pnas.86.18.6838. PMC 297945. PMID 16594069.
