Search results for "Kinetic isotope effects"

showing 5 items of 5 documents

Carboxylate catalyzed isomerization of β,γ‐unsaturated N-acetylcysteamine thioesters

2022

We demonstrate herein the capacity of simple carboxylate salts – tetrametylammonium and tetramethylguanidinium pivalate – to act as catalysts in the isomerization of β,γ-unsaturated thioesters to α,β-unsaturated thioesters. The carboxylate catalysts gave reaction rates comparable to those obtained with DBU, but with fewer side reactions. The reaction exhibits a normal secondary kinetic isotope effect ( k 1H / k 1D = 1.065±0.026) with a β,γ−deuterated substrate. Computational analysis of the mechanism provides a similar value ( k 1H / k 1D = 1.05) with a mechanism where γ-reprotonation of the enolate intermediate is rate determining. peerReviewed

thioesterskatalyytitkinetic isotope effectsisomeriakatalyysirikkiyhdisteetcarboxylatesreaction mechanismreaktiomekanismitbase catalysisisomerizationenolatesorgaaniset yhdisteet
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Why Are Some Enzymes Dimers? Flexibility and Catalysis in Thermotoga maritima Dihydrofolate Reductase

2019

[Image: see text] Dihydrofolate reductase from Thermotoga maritima (TmDFHFR) is a dimeric thermophilic enzyme that catalyzes the hydride transfer from the cofactor NADPH to dihydrofolate less efficiently than other DHFR enzymes, such as the mesophilic analogue Escherichia coli DHFR (EcDHFR). Using QM/MM potentials, we show that the reduced catalytic efficiency of TmDHFR is most likely due to differences in the amino acid sequence that stabilize the M20 loop in an open conformation, which prevents the formation of some interactions in the transition state and increases the number of water molecules in the active site. However, dimerization provides two advantages to the thermophilic enzyme: …

chemistry.chemical_classificationenzyme kinetic isotope effectsbiology010405 organic chemistryStereochemistryChemistryThermophilefree energy calculationsGeneral Chemistry010402 general chemistrybiology.organism_classificationenzyme dimers01 natural sciencesCatalysisCofactor0104 chemical sciencesCatalysisEnzymeDihydrofolate ReductaseThermotoga maritimaDihydrofolate reductasebiology.proteinbacteriaQM/MM methods
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Convergence of Theory and Experiment on the Role of Preorganization, Quantum Tunneling, and Enzyme Motions into Flavoenzyme-Catalyzed Hydride Transfer

2017

Hydride transfer is one of the most common reactions catalyzed by enzymatic systems, and it has become an object of study because of possible significant quantum tunneling effects. In the present work, we provide a combination of theoretical QM/MM simulations and experimental measurements of the rate constants and kinetic isotopic effects (KIEs) for the hydride transfer reaction catalyzed by morphinone reductase, MR. Quantum mechanical tunneling coefficients, computed in the framework of variational transition-state theory, play a significant role in this reaction, reaching values of 23.8 ± 5.5 for the lightest isotopologue—one of the largest values reported for enzymatic systems. This pred…

Morphinone reductase010304 chemical physicsHydrideChemistryThermodynamicsGeneral Chemistry010402 general chemistry01 natural sciencesQM/MMCatalysismolecular dynamicsArticle0104 chemical sciencesReaction coordinateQM/MMMolecular dynamicsReaction rate constantComputational chemistrykinetic isotope effectshydride transfer0103 physical sciencesmorphinone reductaseQuantumQuantum tunnelling
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Theoretical Study of Primary Reaction of Pseudozyma antarctica Lipase B as the Starting Point To Understand Its Promiscuity

2014

Pseudozyma antarctica lipase B (PALB) is a serine hydrolase that catalyzes the hydrolysis of carboxylic acid esters in aqueous medium but it has also shown catalytic activity for a plethora of reactions. This promiscuous activity has found widespread applications. In the present paper, the primary reaction of PALB, its native hydrolytic activity, has been studied using hybrid quantum mechanical/molecular mechanical (QM/MM) potentials. Free energy surfaces, obtained from QM/MM Molecular Dynamics (MD) simulations, show that the reaction takes place by means of a multi-step mechanism where the first step, the activation of the carbonyl group of the substrate and the nucleophilic attack of Ser1…

Candida antarctica lipase BbiologyChemistryStereochemistryHydrolysisEnzyme promiscuityKinetic isotope effectsSubstrate (chemistry)Active siteSerine hydrolaseGeneral ChemistryQM/MMCatalysisCatalysisEnzyme catalysisQM/MMNucleophilebiology.proteinEnzyme promiscuityPseudozyma antarctica lipase BACS Catalysis
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Protein isotope effects in dihydrofolate reductase from Geobacillus stearothermophilus show entropic-enthalpic compensatory effects on the rate const…

2014

Catalysis by dihydrofolate reductase from the moderately thermophilic bacterium Geobacillus stearothermophilus (BsDHFR) was investigated by isotope substitution of the enzyme. The enzyme kinetic isotope effect for hydride transfer was close to unity at physiological temperatures but increased with decreasing temperatures to a value of 1.65 at 5 °C. This behavior is opposite to that observed for DHFR from Escherichia coli (EcDHFR), where the enzyme kinetic isotope effect increased slightly with increasing temperature. These experimental results were reproduced in the framework of variational transition-state theory that includes a dynamical recrossing coefficient that varies with the mass of…

Models MolecularRate constantsStatic ElectricityDihydrofolate reductaseMolecular ConformationThermodynamicsBiochemistryCatalysisCatalysisModerately thermophilicGeobacillus stearothermophilusColloid and Surface ChemistryReaction rate constantDihydrofolate reductaseKinetic isotope effectEscherichia coliGeobacillus stearothermophilusQDTransmission coefficientIncreasing temperaturesCarbon IsotopesbiologyIsotopeNitrogen IsotopesHydrideChemistryKinetic isotope effectsGeneral ChemistryCrystallographyTetrahydrofolate Dehydrogenasebiology.proteinThermodynamicsJournal of the American Chemical Society
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