The enzyme carbamoyl-serine ammonia-lyase (EC 4.3.1.13) catalyzes the chemical reaction

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.

• 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.