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Beta-ureidopropionase

In enzymology, a beta-ureidopropionase () is an enzyme that catalyzes the chemical reaction

N-carbamoyl-beta-alanine + H<sub>2</sub>O beta-alanine + CO<sub>2</sub> + NH<sub>3</sub>

Thus, the two substrates of this enzyme are N-carbamoyl-beta-alanine and H<sub>2</sub>O, whereas its 3 products are beta-alanine, CO<sub>2</sub>, and NH<sub>3</sub>.

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 .

References