L-Dihydroorotic acid
L-Dihydroorotic acid structure
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Common Name | L-Dihydroorotic acid | ||
|---|---|---|---|---|
| CAS Number | 5988-19-2 | Molecular Weight | 158.112 | |
| Density | 1.9±0.1 g/cm3 | Boiling Point | 524.0±60.0 °C at 760 mmHg | |
| Molecular Formula | C5H6N2O4 | Melting Point | 254-255 °C (dec.)(lit.) | |
| MSDS | Chinese USA | Flash Point | 270.7±32.9 °C | |
| Symbol |
GHS07 |
Signal Word | Warning | |
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SEC-TID: A Label-Free Method for Small-Molecule Target Identification.
J. Biomol. Screen. 19(6) , 917-927, (2014) Bioactive small molecules are an invaluable source of therapeutics and chemical probes for exploring biological pathways. Yet, significant hurdles in drug discovery often come from lacking a comprehensive view of the target(s) for both early tool molecules an... |
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The structures of human dihydroorotate dehydrogenase with and without inhibitor reveal conformational flexibility in the inhibitor and substrate binding sites.
Biochemistry 47(34) , 8929-36, (2008) Inhibitors of dihydroorotate dehydrogenase (DHODH) have been suggested for the treatment of rheumatoid arthritis, psoriasis, autoimmune diseases, Plasmodium, and bacterial and fungal infections. Here we present the structures of N-terminally truncated (residu... |
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Miller (Genee-Wiedemann) syndrome represents a clinically and biochemically distinct subgroup of postaxial acrofacial dysostosis associated with partial deficiency of DHODH.
Hum. Mol. Genet. 21(18) , 3969-83, (2012) Biallelic mutations in the gene encoding DHOdehase [dihydroorotate dehydrogenase (DHODH)], an enzyme required for de novo pyrimidine biosynthesis, have been identified as the cause of Miller (Genée-Weidemann or postaxial acrofacial dysostosis) syndrome (MIM 2... |
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Biochemical and molecular characterization of the pyrimidine biosynthetic enzyme dihydroorotate dehydrogenase fromToxoplasma gondii
Mol. Biochem. Parasitol. 184(2) , 71-81, (2012) Graphical abstract Toxoplasma gondii dihydroorotate dehydrogenase is an essential mitochondrial enzyme that exhibits inhibitor sensitivities distinct from those of the human and Plasmodium falciparum enzymes. |
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Site directed spin labeling studies of Escherichia coli dihydroorotate dehydrogenase N-terminal extension.
Biochem. Biophys. Res. Commun. 414(3) , 487-92, (2011) Dihydroorotate dehydrogenases (DHODHs) are enzymes that catalyze the fourth step of the de novo synthesis of pyrimidine nucleotides. In this reaction, DHODH converts dihydroorotate to orotate, using a flavine mononucleotide as a cofactor. Since the synthesis ... |
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Thermodynamic basis of electron transfer in dihydroorotate dehydrogenase B from Lactococcus lactis: analysis by potentiometry, EPR spectroscopy, and ENDOR spectroscopy.
Biochemistry 43(21) , 6498-510, (2004) Dihydroorotate dehydrogenase B (DHODB) is a complex iron-sulfur flavoprotein that catalyzes the conversion of dihydroorotate to orotate and the reduction of NAD(+). The enzyme is a dimer of heterodimers containing an FMN, an FAD, and a 2Fe-2S center. UV-visib... |
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Mutations in yhiT enable utilization of exogenous pyrimidine intermediates in Salmonella enterica serovar Typhimurium.
Microbiology 153(Pt 8) , 2472-82, (2007) Mutants capable of utilizing the pyrimidine biosynthetic intermediates carbamoylaspartate and dihydroorotate for growth were derived from pyrimidine auxotrophs of Salmonella enterica serovar Typhimurium LT2. The gain-of-function phenotypes both resulted from ... |
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Kinetic mechanism and catalysis of Trypanosoma cruzi dihydroorotate dehydrogenase enzyme evaluated by isothermal titration calorimetry.
Anal. Biochem. 399(1) , 13-22, (2010) Trypanosoma cruzi dihydroorotate dehydrogenase (TcDHODH) catalyzes the oxidation of l-dihydroorotate to orotate with concomitant reduction of fumarate to succinate in the de novo pyrimidine biosynthetic pathway. Based on the important need to characterize cat... |
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Mechanism of the dihydroorotase reaction.
Biochemistry 43(51) , 16285-92, (2004) Dihydroorotase (DHO) is a zinc metalloenzyme that functions in the pathway for the biosynthesis of pyrimidine nucleotides by catalyzing the reversible interconversion of carbamoyl aspartate and dihydroorotate. A chemical mechanism was proposed on the basis of... |
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Dihydroorotase from the hyperthermophile Aquifex aeolicus is activated by stoichiometric association with aspartate transcarbamoylase and forms a one-pot reactor for pyrimidine biosynthesis.
Biochemistry 48(4) , 766-78, (2009) In prokaryotes, the first three enzymes in pyrimidine biosynthesis, carbamoyl phosphate synthetase (CPS), aspartate transcarbamoylase (ATC), and dihydroorotase (DHO), are commonly expressed separately and either function independently (Escherichia coli) or as... |