In enzymology, a beta-ureidopropionase () is an enzyme that catalyzes the chemical reaction
N-carbamoyl-beta-alanine + H2O beta-alanine + CO2 + NH3
Thus, the two substrates of this enzyme are N-carbamoyl-beta-alanine and H2O, whereas its 3 products are beta-alanine, CO2, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoyl-beta-alanine amidohydrolase. This enzyme participates in 3 metabolic pathways: pyrimidine metabolism, beta-alanine metabolism, and pantothenate and coenzyme A biosynthesis.
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .