Beta-ureidopropionase

In enzymology, a beta-ureidopropionase (EC 3.5.1.6) is an enzyme that catalyzes the chemical reaction

N-carbamoyl-beta-alanine + H₂O ${\displaystyle \rightleftharpoons }$ 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 1R3N, 1R43, 2V8D, 2V8G, 2V8H, and 2V8V.

References

• CAMPBELL LL (1960). "Reductive degradation of pyrimidines. 5. Enzymatic conversion of N-carbamyl-beta-alanine to beta-alanine, carbon dioxide, and ammonia". J. Biol. Chem. 235: 2375–8. PMID 13849303.
• CARAVACA J, GRISOLIA S (1958). "Enzymatic decarbamylation of carbamyl beta-alanine and carbamyl beta-aminoisobutyric acid". J. Biol. Chem. 231 (1): 357–65. PMID 13538975.
• Traut TW, Loechel S (1984). "Pyrimidine catabolism: individual characterization of the three sequential enzymes with a new assay". Biochemistry. 23 (11): 2533–9. doi:10.1021/bi00306a033. PMID 6433973.

This page was last edited on 26 August 2023, at 13:20