The enzyme carbamoyl-serine ammonia-lyase (EC 4.3.1.13) catalyzes the chemical reaction
| 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 | ||||||||
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- O-carbamoyl-L-serine + H2O = pyruvate + 2 NH3 + CO2 (overall reaction)
- (1a) O-carbamoyl-L-serine = CO2 + NH3 + 2-aminoprop-2-enoate
- (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
- (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
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
edit- 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.
