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Beta-ureidopropionase : ウィキペディア英語版 | Beta-ureidopropionase
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 .
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