L-Dihydroorotic acid has been used as a substrate in dihydroorotate dehydrogenase (DHODH) assay.
500 mg in poly bottle
1, 5 g in poly bottle
L-Dihydroorotic acid (DHO) serves as a substrate for dihydroorotate dehydrogenase (DHODH), an enzyme in the de novo synthesis of pyrimidine. Inhibition of DHOH by its inhibitors causes a large accumulation of upstream metabolite DHO and a reduction in the uridine levels. Therefore, DHO and uridine can be used as biomarkers for pyrimidine synthesis for the clinical development of DHOH inhibitors.
Tandem Mass Spectrometry data independently generated by Scripps Center for Metabolomics is available to view or download in PDF. D7128.pdf Tested metabolites are featured on Scripps Center for Metabolomics METLIN Metabolite Database. To learn more, visit sigma.com/metlin.
Journal of pharmaceutical and biomedical analysis, 192, 113669-113669 (2020-10-30)
Uridine and L-dihydroorotate (DHO) are important intermediates of de novo as well as salvage pathways for the biosynthesis of pyrimidines, which are the building blocks of nucleic acids - DNA and RNA. These metabolites are known to be significant biomarkers
Cell chemical biology, 24(12), 1437-1444 (2017-10-17)
Microbial natural products are genetically encoded by dedicated biosynthetic gene clusters (BGCs). A given BGC usually produces a family of related compounds that share a core but contain variable substituents. Though common, the reasons underlying this divergent biosynthesis are in
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 mutations in a single gene, yhiT, the third gene of
Archives of biochemistry and biophysics, 391(2), 286-294 (2001-07-05)
The flavoprotein dihydroorotate dehydrogenase (DHOD) catalyzes the oxidation of dihydroorotate to orotate. Dihydrooxonate is an analogue of dihydroorotate in which the C5 carbon is substituted by a nitrogen atom. We have investigated dihydrooxonate as a substrate of three DHODs, each
Journal of molecular biology, 348(3), 523-533 (2005-04-14)
Escherichia coli dihydroorotase has been crystallized in the presence of the product, L-dihydroorotate (L-DHO), and the structure refined at 1.9A resolution. The structure confirms that previously reported (PDB entry 1J79), crystallized in the presence of the substrate N-carbamyl-D,L-aspartate (D, L-CA-asp)
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