3.5.1.54	allophanate + H2O	-	CO2 + NH3	-	ir	140567	
3.5.1.54	allophanate + H2O	2nd step in the degradation of urea	CO2 + NH3	-	ir	140567	
3.5.1.54	allophanate + H2O	the enzyme is involved in bacterial cyanuric acid metabolism	NH3 + CO2	-	ir	383056	
3.5.1.54	allophanate + H2O	-	NH3 + CO2	-	ir	383056	
3.5.1.54	allophanate + H2O	the enzyme forms an alternative urea degradation pathway with the urea carboxylase, EC 6.3.4.6	NH3 + CO2	-	ir	383056	
3.5.1.54	allophanate + H2O	-	NH3 + CO2	-	?	383056	
3.5.1.54	allophanate + H2O	the reverse reaction is catalyzed by urea carboxylase	2 CO2 + 2 NH3	-	ir	432652	
3.5.1.54	allophanate + H2O	-	2 CO2 + 2 NH3	-	?	432652	
3.5.1.54	allophanate + H2O	-	2 CO2 + 2 NH3	-	ir	432652	
3.5.1.54	allophanate + H2O	the enzyme exhibits high specificity for allophanate	2 CO2 + 2 NH3	-	?	432652	
3.5.1.54	biuret + H2O	-	?	-	?	384340	
3.5.1.54	malonamic acid + H2O	-	?	-	?	385115	
3.5.1.54	malonamic acid + hydroxylamine	hydroxylamine trapping activity	malonohydroxamate + ?	-	?	385116	
3.5.1.54	malonamide + H2O	-	?	-	?	385117	
3.5.1.54	additional information	allophanate also shows nonenzymatic decomposition, half-life at pH 8.0 is 50 h	?	-	?	89	
3.5.1.54	additional information	substrate specificity, no activity with methyl allophanate, hydantoic acid, oxamic acid, hydroxyurea, methyl carbamate, N-methylurea, acetylurea, 1-acetyl-2-thiourea, and semicarbazide, no activity with rhodanine, rhodanine-3-acetic acid, 3-aminorhodanine, (4R)-(-)-2-thioxo-4-thiazolidinecarboxylic acid, (-)-2-oxo-4-thiazolinecarboxylic acid, and 2-amino-5-bromothiazol	?	-	?	89	
3.5.1.54	additional information	allophanate is produced at the active site of the UC C-terminal domain and is translocated to that of the AH N-domain for subsequent reaction. Allophanate is translocated from the active site of UC C-terminal domain to that of the AH N-domain via diffusion through solvent, instead of being channeled through the dimer	?	-	?	89	
3.5.1.54	additional information	the catalytic reaction is catalyzed by either the full-length AtzF or the amidase domain of AtzF, AtzF467. There is no catalytic advantage conferred by the C terminus of AtzF in vitro	?	-	?	89	
3.5.1.54	additional information	binding process of allophanate to allophanate hydrolase, computational analysis, enzyme-substrate interaction, overview	?	-	?	89	
3.5.1.54	urea-1-carboxylate + H2O	-	2 CO2 + 2 NH3	-	?	449011	
3.5.1.54	urea-1-carboxylate + H2O	-	2 CO2 + 2 NH3	-	r	449011