Carbamoyl-serine ammonia-lyase
| carbamoyl-serine ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.1.13 | ||||||||
| CAS no. | 52227-64-2 | ||||||||
| 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 carbamoyl-serine ammonia-lyase (EC 4.3.1.13) is an enzyme that catalyzes the chemical reaction
- O-carbamoyl-L-serine + H2O pyruvate + 2 NH3 + CO2
Thus, the two substrates of this enzyme are O-carbamoyl-L-serine and H2O, whereas its 3 products are pyruvate, NH3, and CO2.
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is O-carbamoyl-L-serine ammonia-lyase (decarboxylating pyruvate-forming). Other names in common use include O-carbamoyl-L-serine deaminase, carbamoylserine deaminase, and O-carbamoyl-L-serine ammonia-lyase (pyruvate-forming). It employs one cofactor, pyridoxal phosphate.
References
- Copper AJ, Meister A (1973). "Enzymatic conversion of O-carbamyl-L-serine to pyruvate and ammonia". Biochem. Biophys. Res. Commun. 55 (3): 780–7. doi:10.1016/0006-291X(73)91212-6. PMID 4761084.
