EC |
3.5.1.6 |
Accepted name: |
β-ureidopropionase |
Reaction: |
3-ureidopropanoate + H2O = β-alanine + CO2 + NH3 |
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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] |
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[EC 3.5.1.6 created 1961] |
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EC |
3.5.1.95 |
Accepted name: |
N-malonylurea hydrolase |
Reaction: |
3-oxo-3-ureidopropanoate + H2O = malonate + urea |
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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] |
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[EC 3.5.1.95 created 2006] |
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EC |
3.5.2.1 |
Accepted name: |
barbiturase |
Reaction: |
barbiturate + H2O = 3-oxo-3-ureidopropanoate |
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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, PDB, 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] |
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[EC 3.5.2.1 created 1961, modified 2006] |
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EC |
3.5.2.2 |
Accepted name: |
dihydropyrimidinase |
Reaction: |
5,6-dihydrouracil + H2O = 3-ureidopropanoate |
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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] |
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[EC 3.5.2.2 created 1961] |
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