Search results for "Tetrahydrofolate dehydrogenase"

showing 7 items of 17 documents

Chemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate Reductase.

2015

Abstract Chemical ligation has been used to alter motions in specific regions of dihydrofolate reductase from E. coli and to investigate the effects of localized motional changes on enzyme catalysis. Two isotopic hybrids were prepared; one with the mobile N‐terminal segment containing heavy isotopes (2H, 13C, 15N) and the remainder of the protein with natural isotopic abundance, and the other one with only the C‐terminal segment isotopically labeled. Kinetic investigations indicated that isotopic substitution of the N‐terminal segment affected only a physical step of catalysis, whereas the enzyme chemistry was affected by protein motions from the C‐terminal segment. QM/MM studies support th…

Models MolecularTetrahydrofolate Dehydrogenasechemical ligationisotope effectsIsotope LabelingCommunicationprotein dynamicsProtein Dynamics | Very Important PaperLigationenzyme catalysisCatalysisCommunicationsmicroscopic mechanismsAngewandte Chemie (International ed. in English)
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Candidate target mechanisms of the growth inhibitor cyromazine: Studies of phenylalanine hydroxylase, puparial amino acids, and dihydrofolate reducta…

2000

Cyromazine, an insect growth regulator, affects larval and pupal cuticles in dipterans and some other insects. The mode of action of this aminotriazine is not known yet, though it has been shown not to inhibit the synthesis of chitin and cuticular proteins. Cyromazine may, however, act on some step(s) of sclerotization of the cuticle. In the present study, we have analyzed the key enzyme for the production of sclerotization agents, phenylalanine hydroxylase (PAH), using the enzyme from Drosophila, a cyromazine-sensitive insect. PAH was studied in vitro with cyromazine and three biologically less active derivatives at concentrations ranging from 1 μM to 1 mM. None of the compounds did signif…

Phenylalanine hydroxylasePhysiologyCuticlePhenylalanineBiologyBiochemistrychemistry.chemical_compoundHousefliesDihydrofolate reductaseAnimalsAmino AcidsTyrosineMode of actionchemistry.chemical_classificationTriazinesDipterafungiPupaPhenylalanine HydroxylaseGeneral MedicineCyromazineJuvenile HormonesTetrahydrofolate DehydrogenaseDrosophila melanogasterEnzymechemistryBiochemistryInsect Sciencebiology.proteinArchives of Insect Biochemistry and Physiology
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Increased dynamic effects in a catalytically compromised variant of Escherichia coli dihydrofolate reductase

2013

Isotopic substitution (15N, 13C, 2H) of a catalytically compromised variant of Escherichia coli dihydrofolate reductase, EcDHFR-N23PP/S148A, has been used to investigate the effect of these mutations on catalysis. The reduction of the rate constant of the chemical step in the EcDHFR-N23PP/S148A catalyzed reaction is essentially a consequence of an increase of the quasi-classical free energy barrier and to a minor extent of an increased number of recrossing trajectories on the transition state dividing surface. Since the variant enzyme is less well set up to catalyze the reaction, a higher degree of active site reorganization is needed to reach the TS. Although millisecond active site motion…

StereochemistryCoupled motionsKnockoutHydride transferProtein dynamicsChemical stepmedicine.disease_causeTemperature-dependenceBiochemistryCatalysisArticleCatalysisEnzyme catalysisColloid and Surface ChemistryReaction rate constantDihydrofolate reductasemedicineEscherichia coliQDEscherichia colichemistry.chemical_classificationbiologyChemistryProtein dynamicsActive siteEnzyme catalysisGeneral ChemistryTetrahydrofolate DehydrogenaseEnzymeDehydrogenasebiology.proteinBiocatalysisConformational motions
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Are there dynamical effects in enzyme catalysis? Some thoughts concerning the enzymatic chemical step.

2015

Highlights • The possible role of enzymatic reaction dynamical effects is examined. • Solution reactions usefully inform the issue of dynamical effects in enzymes. • Division into regions containing and away from the transition state is important. • Motions in passage to/from the transition state need not lead to dynamical effects. • Transition State Theory is usually a reasonable description of enzyme kinetics.

StereochemistryProtein ConformationBiophysicsBiochemistryModels BiologicalVibrationArticleEnzyme catalysisDiffusionTransition state theoryTransition State TheoryEscherichia coli[CHIM]Chemical SciencesStatistical physicsMolecular BiologyQuantumNuclear motionChemistryQuantitative Biology::Molecular Networksdigestive oral and skin physiologyEnzyme catalysisEnzymesEnzyme ActivationKineticsTetrahydrofolate DehydrogenaseDynamical effectsBiocatalysisQuantum TheoryTetrahydrofolate dehydrogenaseProtonsArchives of biochemistry and biophysics
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Quantifying the limits of transition state theory in enzymatic catalysis

2017

Significance Transition state theory (TST) is the most popular theory to calculate the rates of enzymatic reactions. However, in some cases TST could fail due to the violation of the nonrecrossing hypothesis at the transition state. In the present work we show that even for one of the most controversial enzymatic reactions—the hydride transfer catalyzed by dihydrofolate reductase—the error associated to TST represents only a minor correction to the reaction rate. Moreover, this error is actually larger for the reaction in solution than in the enzymatic active site. Based on this finding and on previous studies we propose an “enzymatic shielding” hypothesis which encompasses various aspects …

Surface (mathematics)enzymatic catalysisDegrees of freedom (statistics)Molecular Dynamics Simulation010402 general chemistry01 natural sciencesEnzyme catalysisReaction coordinateReaction rateTransition state theoryMolecular dynamicsdihydrofolate reductasetransmission coefficientComputational chemistry0103 physical sciencesHumansdynamic effectsStatistical physicsIonsMultidisciplinary010304 chemical physicsChemistryState (functional analysis)Biological Sciencesbacterial infections and mycoses0104 chemical sciencesChemistryBiophysics and Computational BiologyKineticsTetrahydrofolate Dehydrogenasetransition state theoryPhysical SciencesBiocatalysisProceedings of the National Academy of Sciences
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Biopterin metabolism and eNOS expression during hypoxic pulmonary hypertension in mice.

2013

International audience; Tetrahydrobiopterin (BH$_4$), which fosters the formation of and stabilizes endothelial NO synthase (eNOS) as an active dimer, tightly regulates eNOS coupling / uncoupling. Moreover, studies conducted in genetically-modified models demonstrate that BH$_4$ pulmonary deficiency is a key determinant in the pathogenesis of pulmonary hypertension. The present study thus investigates biopterin metabolism and eNOS expression, as well as the effect of sepiapterin (a precursor of BH$_4$) and eNOS gene deletion, in a mice model of hypoxic pulmonary hypertension. In lungs, chronic hypoxia increased BH$_4$ levels and eNOS expression, without modifying dihydrobiopterin (BH$_2$, t…

medicine.medical_specialtySepiapterinNitric Oxide Synthase Type III[SDV]Life Sciences [q-bio]Hypertension PulmonaryBiopterinlcsh:Medicine[SDV.BC]Life Sciences [q-bio]/Cellular Biology[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]030204 cardiovascular system & hematology03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineEnosRight ventricular hypertrophyDihydrobiopterinInternal medicinemedicine[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]AnimalsHypoxialcsh:Science[SDV.BC] Life Sciences [q-bio]/Cellular Biology030304 developmental biology0303 health sciencesMultidisciplinarybiologylcsh:RHypoxia (medical)biology.organism_classificationmedicine.diseasePulmonary hypertensionBiopterin[SDV] Life Sciences [q-bio]Disease Models AnimalTetrahydrofolate DehydrogenaseEndocrinologychemistryVentricular pressurelcsh:Qmedicine.symptomResearch ArticlePLoS ONE
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Effect of genetic polymorphisms involved in folate metabolism on the concentration of serum folate and plasma total homocysteine (p-tHcy) in healthy …

2015

Data on the effect of combined genetic polymorphisms, involved in folate metabolism, on the concentration of serum folate after folic acid supplementation are scarce. Therefore, we investigated the impact of seven gene polymorphisms on the concentration of serum folate and p-tHcy in healthy subjects after short-term folic acid supplementation. In a randomized, double blind, crossover study, apparently healthy subjects were given either 0.8 mg folic acid per day (n = 46) or placebo (n = 45) for 14 days. The washout period was 14 days. Fasting blood samples were collected on day 1, 15, 30 and 45. Data on subjects on folic acid supplementation (n = 91) and on placebo (n = 45) were used for the…

medicine.medical_specialtybiologybusiness.industryEndocrinology Diabetes and MetabolismClinical nutritionPlaceboCrossover studyFolic acid supplementationDouble blindEndocrinologyBiochemistryPolymorphism (computer science)Internal medicineMethylenetetrahydrofolate reductaseMethylenetetrahydrofolate dehydrogenaseGeneticsmedicinebiology.proteinbusinessResearch Paper
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