Enzymes
| UniProtKB help_outline | 505 proteins |
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- Name help_outline barbiturate Identifier CHEBI:77938 Charge -1 Formula C4H3N2O3 InChIKeyhelp_outline GVLZYMDNTPNTLV-UHFFFAOYSA-N SMILEShelp_outline O=c1[cH-]c(=O)[nH]c(=O)[nH]1 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-oxo-3-ureidopropanoate Identifier CHEBI:58775 Charge -1 Formula C4H5N2O4 InChIKeyhelp_outline UCUUMUFWVSUBOL-UHFFFAOYSA-M SMILEShelp_outline NC(=O)NC(=O)CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:18653 | RHEA:18654 | RHEA:18655 | RHEA:18656 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase.
Soong C.-L., Ogawa J., Shimizu S.
Amidohydrolytic reactions in oxidative pyrimidine metabolism were investigated in detail. Barbiturase has been reported to catalyze the amidohydrolysis of barbituric acid to urea and malonic acid. However, purification of the enzyme revealed that it catalyzes the ring-opening of barbituric acid to ... >> More
Amidohydrolytic reactions in oxidative pyrimidine metabolism were investigated in detail. Barbiturase has been reported to catalyze the amidohydrolysis of barbituric acid to urea and malonic acid. However, purification of the enzyme revealed that it catalyzes the ring-opening of barbituric acid to ureidomalonic acid. The existence of a consecutive enzyme named ureidomalonase, which hydrolyzes ureidomalonic acid to urea and malonic acid, was also discovered during the purification of barbiturase. << Less
Biochem. Biophys. Res. Commun. 286:222-226(2001) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism.
Soong C.-L., Ogawa J., Sakuradani E., Shimizu S.
Barbiturase, which catalyzes the reversible amidohydrolysis of barbituric acid to ureidomalonic acid in the second step of oxidative pyrimidine degradation, was purified to homogeneity from Rhodococcus erythropolis JCM 3132. The characteristics and gene organization of barbiturase suggested that i ... >> More
Barbiturase, which catalyzes the reversible amidohydrolysis of barbituric acid to ureidomalonic acid in the second step of oxidative pyrimidine degradation, was purified to homogeneity from Rhodococcus erythropolis JCM 3132. The characteristics and gene organization of barbiturase suggested that it is a novel zinc-containing amidohydrolase that should be grouped into a new family of the amidohydrolases superfamily. The amino acid sequence of barbiturase exhibited 48% identity with that of herbicide atrazine-decomposing cyanuric acid amidohydrolase but exhibited no significant homology to other proteins, indicating that cyanuric acid amidohydrolase may have evolved from barbiturase. A putative uracil phosphoribosyltransferase gene was found upstream of the barbiturase gene, suggesting mutual interaction between pyrimidine biosynthesis and oxidative degradation. Metal analysis with an inductively coupled radiofrequency plasma spectrophotometer revealed that barbiturase contains approximately 4.4 mol of zinc per mol of enzyme. The homotetrameric enzyme had K(m) and V(max) values of 1.0 mm and 2.5 micromol/min/mg of protein, respectively, for barbituric acid. The enzyme specifically acted on barbituric acid, and dihydro-l-orotate, alloxan, and cyanuric acid competitively inhibited its activity. The full-length gene encoding the barbiturase (bar) was cloned and overexpressed in Escherichia coli. The kinetic parameters and physicochemical properties of the cloned enzyme were apparently similar to those of the wild-type. << Less
J. Biol. Chem. 277:7051-7058(2002) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.