In enzymology, a gamma-glutamylcyclotransferase (EC 2.3.2.4) is an enzyme that catalyzes the chemical reaction
| gamma-glutamylcyclotransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.2.4 | ||||||||
| CAS no. | 9045-44-7 | ||||||||
| 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 | ||||||||
| |||||||||
- (5-L-glutamyl)-L-amino acid 5-oxoproline + L-amino acid
Hence, this enzyme has one substrate, (5-L-glutamyl)-L-amino acid, and two products, 5-oxoproline and L-amino acid.
This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. The systematic name of this enzyme class is (5-L-glutamyl)-L-amino-acid 5-glutamyltransferase (cyclizing). Other names in common use include gamma-glutamyl-amino acid cyclotransferase, gamma-L-glutamylcyclotransferase, and L-glutamic cyclase. This enzyme participates in glutathione metabolism.
Structural studies
editAs of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2PN7 and 2RBH.
References
edit- Bodnaryk RP; McGirr L (1973). "Purification, properties and function of a unique gamma-glutamyl cyclotransferase from the housefly, Musca domestica L". Biochim. Biophys. Acta. 315 (2): 352–362. doi:10.1016/0005-2744(73)90264-7.
- Orlowski M, Richman PG, Meister A (1969). "Isolation and properties of gamma-L-glutamylcyclotransferase from human brain". Biochemistry. 8 (3): 1048–1055. doi:10.1021/bi00831a036. PMID 5781001.
