In enzymology, a dihydropyrimidinase () is an enzyme that catalyzes the chemical reaction 5,6-dihydrouracil + H2O 3-ureidopropanoate Thus, the two substrates of this enzyme are 5,6-dihydrouracil and H2O, whereas its product is 3-ureidopropanoate. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 5,6-dihydropyrimidine amidohydrolase. Other names in common use include hydantoinase, hydropyrimidine hydrase, hydantoin peptidase, pyrimidine hydrase, and D-hydantoinase. This enzyme participates in 3 metabolic pathways: pyrimidine metabolism, beta-alanine metabolism, and pantothenate and coa biosynthesis. Structural studies As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , and . References EC 3.5.2 Enzymes of known structure