Dihydroorotate Dehydrogenase
Mostrando 1-12 de 28 artigos, teses e dissertações.
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1. Planejamento de inibidores das enzimas diidroorotato desidrogenase de Trypanosoma cruzi e Leishmania major / Design of inhibitors for dihydroorotate dehydrogenase from Trypanosoma cruzi and Leishmania major
Dihydroorotate dehydrogenase (DHODH) catalyses the conversion of dihydroorote to orotate, the fourth step and only redox reaction in the de novo pyrimidine biosynthetic pathway. DHODH has been exploited as a validated target for therapy against proliferative and parasitic diseases, and in particular, has been considered to be an attractive target for drug de
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 25/04/2012
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2. Planejamento de inibidores da enzima diidroorotato desidrogenase de Trypanosoma cruzi por biocalorimetria / Biocalorimetry as a tool for Trypanosoma cruzi dihydroorotate dehydrogenase inhibitors discovery
A doença de Chagas, causada pelo protozoário flagelado Trypanosoma cruzi, é uma doença tropical que enseja morte/morbidade de milhões de pessoas na América Latina. Por processos migratórios, vem-se estendendo ao sul dos Estados Unidos, Canadá, Europa, Austrália e Japão. Essa doença tem sido considerada super-negligenciada pela indústria farmacêu
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 04/03/2011
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3. Identification of a novel gene of pyrimidine nucleotide biosynthesis, pyrDII, that is required for dihydroorotate dehydrogenase activity in Bacillus subtilis.
An in-frame deletion in the coding region of a gene of previously unidentified function (which is called orf2 and which we propose to rename pyrDII) in the Bacillus subtilis pyr operon led to pyrimidine bradytrophy, markedly reduced dihydroorotate dehydrogenase activity, and derepressed levels of other enzymes of pyrimidine biosynthesis. The deletion mutatio
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4. Two different dihydroorotate dehydrogenases in Lactococcus lactis.
The pyrimidine de novo biosynthesis pathway has been characterized for a number of organisms. The general pathway consists of six enzymatic steps. In the characterization of the pyrimidine pathway of Lactococcus lactis, two different pyrD genes encoding dihydroorotate dehydrogenase were isolated. The nucleotide sequences of the two genes, pyrDa and pyrDb, ha
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5. Biosynthetic Dihydroorotate Dehydrogenase from Lactobacillus bulgaricus: Partial Characterization of the Enzyme
Some of the catalytic properties of the biosynthetic dihydroorotate dehydrogenase purified from an anaerobic bacterium, Lactobacillus bulgaricus, are described. Studies with p-hydroxymercuribenzoate, N-ethylmaleimide, and mercuric chloride showed that sulfhydryl groups are necessary for transfer of electrons from dihydroorotate to a variety of electron accep
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6. ENZYMES OF THE PYRIMIDINE PATHWAY IN ESCHERICHIA COLI I. : Synthesis by Cells and Spheroplasts
Taylor, W. Herman (Portland State College, Portland, Ore.), and G. David Novelli. Enzymes of the pyrimidine pathway in Escherichia coli. I. Synthesis by cells and spheroplasts. J. Bacteriol. 88:99–104. 1964.—Upon release from repression, cells and spheroplasts of two mutants of Escherichia coli efficiently synthesized aspartate transcarbamylase and ornit
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7. Biosynthetic Dihydroorotate Dehydrogenase from Lactobacillus bulgaricus
This paper describes the first detailed study on a dihydroorotate dehydrogenase involved in pyrimidine biosynthesis. In most organisms the enzyme is membrane-bound; however, a soluble dihydroorotate dehydrogenase was produced in relatively high levels when the anaerobe, Lactobacillus bulgaricus, was released from repression. The enzyme was purified 213-fold
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8. Cloning of the URA1 gene of Saccharomyces cerevisiae.
A 5.7-kilobase segment of Saccharomyces cerevisiae deoxyribonucleic acid which complements both the yeast ura1 and Escherichia coli pyrD mutations in dihydroorotate dehydrogenase has been cloned in plasmid YRp7.
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9. Effects of atovaquone and other inhibitors on Pneumocystis carinii dihydroorotate dehydrogenase.
Dihydroorotate dehydrogenase (DHOD) is a pyrimidine biosynthetic enzyme which is usually directly linked to the mitochondrial respiratory chain. Antimalarial naphthoquinones such as atovaquone (566c80) inhibit malarial DHOD by inhibiting electron transport. Since atovaquone also has therapeutic activity against Pneumocystis carinii, the P. carinii DHOD may a
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10. Sequence analysis and identification of the pyrKDbF operon from Lactococcus lactis including a novel gene, pyrK, involved in pyrimidine biosynthesis.
Three genes encoding enzymes involved in the biosynthesis of pyrimidines have been found to constitute an operon in Lactococcus lactis. Two of the genes are the well-known pyr genes pyrDb and pyrF, encoding dihydroorotate dehydrogenase and orotidine monophosphate decarboxylase, respectively. The third gene encodes a protein which was shown to be necessary fo
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11. Structural Plasticity of Malaria Dihydroorotate Dehydrogenase Allows Selective Binding of Diverse Chemical Scaffolds*
Malaria remains a major global health burden and current drug therapies are compromised by resistance. Plasmodium falciparum dihydroorotate dehydrogenase (PfDHODH) was validated as a new drug target through the identification of potent and selective triazolopyrimidine-based DHODH inhibitors with anti-malarial activity in vivo. Here we report x-ray structure
American Society for Biochemistry and Molecular Biology.
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12. Immunochemical analysis of inner and outer membranes of Escherichia coli by crossed immunoelectrophoresis.
Isolated membrane fractions of Escherichia coli K-12 yielded complex immunoprecipitate patterns when Triton X-100 and sodium dodecyl sulfate extracts were examined by crossed immunoelectrophoresis with antienvelope immunoglobulins. Twelve of the 46 antigens in the immunoprecipitate patterns of inner (plasma) membranes were identified by zymograms and/or by t