N-malonylurea hydrolase

From Wikipedia, the free encyclopedia

In enzymology, a N-malonylurea hydrolase (EC 3.5.1.95) is an enzyme that catalyzes the chemical reaction

3-oxo-3-ureidopropanoate + H₂O malonate + urea

Thus, the two substrates of this enzyme are 3-oxo-3-ureidopropanoate and H₂O, whereas its two products are malonate and urea.

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 3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate-forming). This enzyme is also called ureidomalonase.

[edit] References

• IUBMB entry for 3.5.1.95
• BRENDA references for 3.5.1.95 (Recommended.)
• PubMed references for 3.5.1.95
• PubMed Central references for 3.5.1.95
• Google Scholar references for 3.5.1.95
• Soong CL, Ogawa J, Shimizu S (2001). "Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase". Biochem. Biophys. Res. Commun. 286: 222–6. doi:10.1006/bbrc.2001.5356. PMID 11485332. 
• Soong CL, Ogawa J, Sakuradani E, Shimizu S (2002). "Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism". J. Biol. Chem. 277: 7051–8. doi:10.1074/jbc.M110784200. PMID 11748240. 

[edit] External links

• IUBMB entry for 3.5.1.95

• KEGG entry for 3.5.1.95

• BRENDA entry for 3.5.1.95

• NiceZyme view of 3.5.1.95

• EC2PDB: PDB structures for 3.5.1.95

• PRIAM entry for 3.5.1.95

• PUMA2 entry for 3.5.1.95

• IntEnz: Integrated Enzyme entry for 3.5.1.95

• MetaCyc entry for 3.5.1.95

• Atomic-resolution structures of enzymes belonging to this class