Pteridine Reductase
Mostrando 1-12 de 15 artigos, teses e dissertações.
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1. DETERMINAÇÃO E ESTUDOS DE ESTRUTURAS DE COMPLEXOS ENZIMALIGANTES RELEVANTES À BIOLOGIA DAS PTERIDINAS EM PARASITAS: BASE PARA O DESENVOLVIMENTO RACIONAL DE DROGAS TERAPÊUTICAS CONTRA DOENÇA DO SONO
As enzimas dihidrofolato redutase-timidilato sintase (DHFR-TS) e pteridina redutase (PTR) estão envolvidas no metabolismo pterina/folato dependente; juntas, representam um importante alvo para a quimioterapia de leishmanias e tripanossomas parasitas. A Cristalografia por Raios X foi utilizada para elucidar acuradamente a estrutura da enzima PTR1 de Trypanos
Publicado em: 2007
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2. PTR1: a reductase mediating salvage of oxidized pteridines and methotrexate resistance in the protozoan parasite Leishmania major.
Trypanosomatid protozoans are pterin auxotrophs, a finding noted decades ago which heralded the discovery of key metabolic roles played by pteridines in eukaryotes. We have now identified the enzyme mediating unconjugated pteridine salvage in the human parasite Leishmania major, PTR1 (pteridine reductase 1, formerly hmtxr or ltdh). PTR1 is the gene in the am
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3. Probing the salt bridge in the dihydrofolate reductase-methotrexate complex by using the coordinate-coupled free-energy perturbation method.
The importance of the ionic interaction due to the formation of the salt bridge between the Asp-27 and the pteridine ring in Escherichia coli dihydrofolate reductase-methotrexate complex has been studied by using the free-energy perturbation method. The calculation suggests that the ion-pair contribution to the binding energy is insignificant, as the enzyme
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4. FolM, A New Chromosomally Encoded Dihydrofolate Reductase in Escherichia coli
Escherichia coli (thyA ΔfolA) mutants are viable and can grow in minimal medium when supplemented with thymidine alone. Here we present evidence from in vivo and in vitro studies that the ydgB gene determines an alternative dihydrofolate reductase that is related to the trypanosomatid pteridine reductases. We propose to rename this gene folM.
American Society for Microbiology.
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5. Phenylketonuric Tetrahymena: phenylalanine hydroxylase mutants and other tyrosine auxotrophs.
Nineteen tyrosine auxotrophs of the ciliated protozoan Tetrahymena thermophila have been isolated and biochemically examined. These mutants are defective in the conversion of phenylalanine to tyrosine; this is analogous to the defect that causes phenylketonuria in humans. After nitrosoguanidine mutagenesis and self-fertilization, progeny clones were screened
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6. Dihydropteridine Reductase as an Alternative to Dihydrofolate Reductase for Synthesis of Tetrahydrofolate in Thermus thermophilus
A strategy devised to isolate a gene coding for a dihydrofolate reductase from Thermus thermophilus DNA delivered only clones harboring instead a gene (the T. thermophilus dehydrogenase [DHTt] gene) coding for a dihydropteridine reductase which displays considerable dihydrofolate reductase activity (about 20% of the activity detected with 6,7-dimethyl-7,8-di
American Society for Microbiology.
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7. Isolation and characterization of dihydropteridine reductase from Pseudomonas species.
Dihydropteridine reductase isolated from the bacterium Pseudomonas species (ATCC 11299a) has been purified approximately 450-fold byammonium sulfate precipitation and diethylaminoethyl-cellulose chromatographic procedures. The preparation is at least 80% pure as judged by polyacrylamide gels. Its molecular weight was determined to be about 44,000. Both dihyd
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8. Isolation and expression of rat liver sepiapterin reductase cDNA.
Sepiapterin reductase (7,8-dihydrobiopterin: NADP+ oxidoreductase, EC 1.1.1.153) catalyzes the terminal step in the biosynthetic pathway for tetrahydrobiopterin, the cofactor necessary for aromatic amino acid hydroxylation. We report here the isolation of a cDNA clone for rat liver sepiapterin reductase. The cDNA has been excised from a lambda vector and the
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9. Dihydrofolate Reductases in Some Folate-Requiring Bacteria with Low Trimethoprim Susceptibility
Dihydrofolate reductases from the folate-requiring strains Streptococcus faecalis ATCC 8043, Lactobacillus casei ATCC 7496, and Pediococcus cerevisiae ATCC 8081, as well as from Lactobacillus arabinosus, which is not dependent on exogenous folate, were isolated, and their properties were compared to reductases of Escherichia coli B, Staphylococcus aureus, an
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10. Inhibition of Folate Enzymes by Sulfasalazine
Sulfasalazine (salicylazosulfapyridine), an agent widely used for the treatment of ileitis and colitis, is also a competitive inhibitor of intestinal folate transport (1, 2). The mechanism of action of sulfasalazine remains uncertain. To further explore the mechanism of sulfasalazine action, the interaction of the drug with the folate recognition site was te
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11. Antimycobacterial Activities of 2,4-Diamino-5-Deazapteridine Derivatives and Effects on Mycobacterial Dihydrofolate Reductase
Development of new antimycobacterial agents for Mycobacterium avium complex (MAC) infections is important particularly for persons coinfected with human immunodeficiency virus. The objectives of this study were to evaluate the in vitro activity of 2,4-diamino-5-methyl-5-deazapteridines (DMDPs) against MAC and to assess their activities against MAC dihydrofol
American Society for Microbiology.
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12. Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer.
Nitric oxide synthases (NOSs), which catalyze the formation of the ubiquitous biological messenger molecule nitric oxide, represent unique cytochrome P-450s, containing reductase and mono-oxygenase domains within one polypeptide and requiring tetrahydrobiopterin as cofactor. To investigate whether tetrahydrobiopterin functions as an allosteric effector of NO