Carbamoyl-serine ammonia-lyase

In enzymology, a carbamoyl-serine ammonia-lyase is an enzyme that catalyzes the chemical reaction


 * O-carbamoyl-L-serine + H2O $$\rightleftharpoons$$ 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.