Gamma-glutamylcyclotransferase
| 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 | ||||||||
| |||||||||
In enzymology, a gamma-glutamylcyclotransferase (EC 2.3.2.4) is an enzyme that catalyzes the chemical reaction
- (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
[edit]As 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.
