The Enzyme Database

Your query returned 4 entries.    printer_iconPrintable version



EC 1.1.99.19      
Transferred entry: uracil dehydrogenase. Now EC 1.17.99.4, uracil/thymine dehydrogenase
[EC 1.1.99.19 created 1961 as EC 1.2.99.1, transferred 1984 to EC 1.1.99.19, deleted 2006]
 
 
EC 1.17.99.4     
Accepted name: uracil/thymine dehydrogenase
Reaction: (1) uracil + H2O + acceptor = barbiturate + reduced acceptor
(2) thymine + H2O + acceptor = 5-methylbarbiturate + reduced acceptor
For diagram of pyrimidine catabolism, click here
Other name(s): uracil oxidase; uracil-thymine oxidase; uracil dehydrogenase
Systematic name: uracil:acceptor oxidoreductase
Comments: Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 3.5.2.1 (barbiturase) and EC 3.5.1.95 (N-malonylurea hydrolase). Mammals, plants and other microorganisms utilize the reductive pathway, comprising EC 1.3.1.1 [dihydrouracil dehydrogenase (NAD+)] or EC 1.3.1.2 [dihydropyrimidine dehydrogenase (NADP+)], EC 3.5.2.2 (dihydropyrimidinase) and EC 3.5.1.6 (β-ureidopropionase), with the ultimate degradation products being an L-amino acid, NH3 and CO2 [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-00-9
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.  Wang, T.P. and Lampen, J.O. Metabolism of pyrimidines by a soil bacterium. J. Biol. Chem. 194 (1952) 775–783. [PMID: 14927671]
3.  Wang, T.P. and Lampen, J.O. Uracil oxidase and the isolation of barbituric acid from uracil oxidation. J. Biol. Chem. 194 (1952) 785–791. [PMID: 14927672]
4.  Lara, F.J.S. On the decomposition of pyrimidines by bacteria. II. Studies with cell-free enzyme preparations. J. Bacteriol. 64 (1952) 279–285. [PMID: 14955523]
5.  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]
[EC 1.17.99.4 created 1961 as EC 1.2.99.1, transferred 1984 to EC 1.1.99.19, transferred 2006 to EC 1.17.99.4]
 
 
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 3.5.2.13     
Accepted name: 2,5-dioxopiperazine hydrolase
Reaction: 2,5-dioxopiperazine + H2O = glycylglycine
Other name(s): cyclo(Gly-Gly) hydrolase; cyclo(glycylglycine) hydrolase
Systematic name: 2,5-dioxopiperazine amidohydrolase
Comments: Highly specific; does not hydrolyse other dioxopiperazines, glycylglycine, proteins or barbiturates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 97599-45-6
References:
1.  Suzuki, Y. and Uchida, K. Multiple forms of α-glycosidase from pig duodenum. Agric. Biol. Chem. 49 (1985) 1573–1581.
[EC 3.5.2.13 created 1989]
 
 


Data © 2001–2020 IUBMB
Web site © 2005–2020 Andrew McDonald