2.7.2.2	ATP + carbamate = ADP + carbamoyl phosphate	(1a)	-	
2.7.2.2	ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O	comparison of carbamate kinases and carbamoyl phosphate synthases	642233	
2.7.2.2	ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O	mechanism	-, 642219, 642223, 642225, 642226, 642229	
2.7.2.2	ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O	overall reaction	-	
2.7.2.2	ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O	random type reaction mechanism	642221	
2.7.2.2	ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O	the protein residues involved in ligand binding, together with a model of the transition state, suggest that catalysis follows an in-line, predominantly dissociative, phosphotransfer reaction mechanism, and that closure of the flexible auxiliary domain is required to protect the transition state from bulk solvent. Model of the transition state, overview	739466	
2.7.2.2	NH3 + hydrogencarbonate = carbamate + H2O	(1b), spontaneous	-