Beta-ureidopropionase
| Beta-ureidopropionase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.6 | ||||||||
| CAS no. | 9027-27-4 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Beta-ureidopropionase (EC 3.5.1.6) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from rat liver hydrolyses 3-ureidopropionic acid to β-alanine, with ammonia and carbon dioxide as byproducts.[1][2][3] In humans, the reaction is part of the breakdown of pyrimidines.[4][5]
This enzyme is a hydrolase, one 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.[6]
Structural studies
[edit]As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1R3N, PDB: 1R43, PDB: 2V8D, PDB: 2V8G, PDB: 2V8H, and PDB: 2V8V.
References
[edit]- ↑ Caravaca J, Grisolia S (1958). "Enzymatic decarbamylation of carbamyl beta-alanine and carbamyl beta-aminoisobutyric acid". J. Biol. Chem. 231 (1): 357–65. doi:10.1016/S0021-9258(19)77312-8. PMID 13538975.
- ↑ 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. doi:10.1016/S0021-9258(18)64630-7. PMID 13849303.
- ↑ 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.
- ↑ Maurer, Dirk; Lohkamp, Bernhard; Krumpel, Michael; Widersten, Mikael; Dobritzsch, Doreen (2018). "Crystal structure and pH-dependent allosteric regulation of human β-ureidopropionase, an enzyme involved in anticancer drug metabolism". Biochemical Journal. 475 (14): 2395–2416. doi:10.1042/BCJ20180222. PMID 29976570.
- ↑ Boča, Roman; Rádiková, Žofia; Štofko, Juraj; Vranovičová, Beata; Rajnák, Cyril (2025). "Quantum chemical study of molecular properties of small branched-chain amino acids in water". Amino Acids. 57 (1) 11. doi:10.1007/s00726-024-03437-y. PMC 11743389. PMID 39827427.
- ↑ Enzyme 3.5.1.6 at KEGG Pathway Database.
