| N2-(2-carboxyethyl)arginine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.66 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a N2-(2-carboxyethyl)arginine synthase (EC 2.5.1.66) is an enzyme that catalyzes the chemical reaction
- D-glyceraldehyde 3-phosphate + L-arginine N2-(2-carboxyethyl)-L-arginine + phosphate
Thus, the two substrates of this enzyme are D-glyceraldehyde 3-phosphate and L-arginine, whereas its two products are N2-(2-carboxyethyl)-L-arginine and phosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is glyceraldehyde-3-phosphate:L-arginine N2-(2-hydroxy-3-oxopropyl) transferase (2-carboxyethyl-forming). Other names in common use include CEAS, N2-(2-carboxyethyl)arginine synthetase, CEA synthetase, glyceraldehyde-3-phosphate:L-arginine 2-N-(2-hydroxy-3-oxopropyl), and transferase (2-carboxyethyl-forming). This enzyme participates in clavulanic acid biosynthesis.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2IHT and 2IHV.
References
- Caines ME, Elkins JM, Hewitson KS, Schofield CJ (2004). "Crystal structure and mechanistic implications of N2-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway". J. Biol. Chem. 279 (7): 5685–92. doi:10.1074/jbc.M310803200. PMID 14623876.
- Khaleeli N; Li R; Townsend CA (1999). "Origin of the beta-lactam carbons in clavulanic acid from an unusual thiamine pyrophosphate-mediated reaction". J. Am. Chem. Soc. 121 (39): 9223–9224. doi:10.1021/ja9923134.