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Dihydropyrimidinase

In enzymology, a dihydropyrimidinase (EC 3.5.2.2) is an enzyme that catalyzes the chemical reaction In enzymology, a dihydropyrimidinase (EC 3.5.2.2) is an enzyme that catalyzes the chemical reaction 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. As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1GKP, 1GKQ, 1GKR, 1NFG, 1YNY, 2FTW, 2FTY, 2FVK, 2FVM, and 2GSE.

[ "Gene", "Substrate (chemistry)", "Enzyme", "Amino acid", "Bacteria", "D-carbamoylase", "Hydantoinase activity", "Dihydropyrimidinase activity", "DIHYDROPYRIMIDINASE DEFICIENCY", "N-carbamoyl-D-amino acid hydrolase" ]
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