The Enzyme Database

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EC 3.5.1.6     
Accepted name: β-ureidopropionase
Reaction: 3-ureidopropanoate + H2O = β-alanine + CO2 + NH3
For diagram of pyrimidine catabolism, click here
Glossary: 3-ureidopropanoate = N-carbamoyl-β-alanine
Other name(s): N-carbamoyl-β-alanine amidohydrolase
Systematic name: 3-ureidopropanoate amidohydrolase
Comments: The animal enzyme also acts on β-ureidoisobutyrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-27-4
References:
1.  Campbell, L.L. Reductive degradation of pyrimidines. 5. Enzymatic conversion of N-carbamyl-β-alanine to β-alanine, carbon dioxide, and ammonia. J. Biol. Chem. 235 (1960) 2375–2378. [PMID: 13849303]
2.  Caravaca, J. and Grisolia, S. Enzymatic decarbamylation of carbamyl β-alanine and carbamyl β-aminoisobutyric acid. J. Biol. Chem. 231 (1958) 357–365. [PMID: 13538975]
3.  Traut, T.W. and Loechel, S. Pyrimidine catabolism: individual characterization of the three sequential enzymes with a new assay. Biochemistry 23 (1984) 2533–2539. [PMID: 6433973]
[EC 3.5.1.6 created 1961]
 
 
EC 3.5.1.95     
Accepted name: N-malonylurea hydrolase
Reaction: 3-oxo-3-ureidopropanoate + H2O = malonate + urea
For pyrimidine catabolism, click here
Other name(s): ureidomalonase
Systematic name: 3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate-forming)
Comments: Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.2.1 (barbiturase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 368888-22-6
References:
1.  Soong, C.L., Ogawa, J. and Shimizu, S. Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase. Biochem. Biophys. Res. Commun. 286 (2001) 222–226. [DOI] [PMID: 11485332]
2.  Soong, C.L., Ogawa, J., Sakuradani, E. and Shimizu, S. Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism. J. Biol. Chem. 277 (2002) 7051–7058. [DOI] [PMID: 11748240]
[EC 3.5.1.95 created 2006]
 
 
EC 3.5.2.1     
Accepted name: barbiturase
Reaction: barbiturate + H2O = 3-oxo-3-ureidopropanoate
For diagram of pyrimidine catabolism, click here
Glossary: barbiturate = 6-hydroxyuracil
Systematic name: barbiturate amidohydrolase (3-oxo-3-ureidopropanoate-forming)
Comments: Contains zinc and is specific for barbiturate as substrate [3]. Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.1.95 (N-malonylurea hydrolase). It was previously thought that the end-products of the reaction were malonate and urea but this has since been disproved [2]. May be involved in the regulation of pyrimidine metabolism, along with EC 2.4.2.9, uracil phosphoribosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-16-5
References:
1.  Hayaishi, O. and Kornberg, A. Metabolism of cytosine, thymine, uracil, and barbituric acid by bacterial enzymes. J. Biol. Chem. 197 (1952) 717–723. [PMID: 12981104]
2.  Soong, C.L., Ogawa, J. and Shimizu, S. Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase. Biochem. Biophys. Res. Commun. 286 (2001) 222–226. [DOI] [PMID: 11485332]
3.  Soong, C.L., Ogawa, J., Sakuradani, E. and Shimizu, S. Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism. J. Biol. Chem. 277 (2002) 7051–7058. [DOI] [PMID: 11748240]
[EC 3.5.2.1 created 1961, modified 2006]
 
 
EC 3.5.2.2     
Accepted name: dihydropyrimidinase
Reaction: 5,6-dihydrouracil + H2O = 3-ureidopropanoate
For diagram of pyrimidine catabolism, click here
Other name(s): hydantoinase; hydropyrimidine hydrase; hydantoin peptidase; pyrimidine hydrase; D-hydantoinase
Systematic name: 5,6-dihydropyrimidine amidohydrolase
Comments: Also acts on dihydrothymine and hydantoin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9030-74-4
References:
1.  Brooks, K.P., Jones, E.A., Kim, B.-D. and Sander, E.G. Bovine liver dihydropyrimidine amidohydrolase: purification, properties, and characterization as a zinc metalloenzyme. Arch. Biochem. Biophys. 226 (1983) 469–483. [DOI] [PMID: 6639068]
2.  Eadie, G.S., Bernheim, F. and Bernheim, J.L.C. Metabolism of cytosine, thymidine, uracil and barbituric acid by bacterial enzymes. J. Biol. Chem. 181 (1949) 449–458. [PMID: 15393763]
[EC 3.5.2.2 created 1961]
 
 


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