2000
Energetics of S-Adenosylmethionine Synthetase Catalysis †
McQueney M, Anderson K, Markham G. Energetics of S-Adenosylmethionine Synthetase Catalysis †. Biochemistry 2000, 39: 4443-4454. PMID: 10757994, DOI: 10.1021/bi992876s.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceBinding SitesCatalysisComputer SimulationDiphosphatesEscherichia coliFluorescenceHydrolysisIsomerismKineticsLigandsMethionineMethionine AdenosyltransferaseOxygenOxygen IsotopesPhosphatesPolyphosphatesS-AdenosylmethionineSolventsThermodynamicsTitrimetryWaterConceptsFree energy profilesSubstrate bindingLoop movementEnergy profilesFormation of AdoMetS-adenosylmethionineChemical interconversion stepPre-steady-state kineticsS-adenosylmethionine synthetaseProduct releaseP(i) complexEquilibrium binding measurementsEnzyme-catalyzed reactionsAdoMet formationBiological alkylating agentsConcentration of substrateFormation reactionCrystallographic studiesEnzyme turnoverEquilibrium constantsCatalyze formationRate constantsInterconversion stepActive siteBinding energy
1998
Kinetic Reaction Scheme for the Dihydrofolate Reductase Domain of the Bifunctional Thymidylate Synthase−Dihydrofolate Reductase from Leishmania major †
Liang P, Anderson K. Kinetic Reaction Scheme for the Dihydrofolate Reductase Domain of the Bifunctional Thymidylate Synthase−Dihydrofolate Reductase from Leishmania major †. Biochemistry 1998, 37: 12206-12212. PMID: 9724534, DOI: 10.1021/bi9803170.Peer-Reviewed Original ResearchConceptsThymidylate synthase-dihydrofolate reductaseKinetic reaction schemeCatalytic activityDihydrofolate reductaseBifunctional enzymeReaction schemeBifunctional thymidylate synthase-dihydrofolate reductaseE. coli enzymeSynthase-dihydrofolate reductaseSteady-state turnoverDihydrofolate reductase domainState kinetic methodsSingle polypeptide chainEnzyme dihydrofolate reductaseSpecies of protozoaReaction pathwaysRelease of productsColi enzymeParasite Leishmania majorMonofunctional formsDihydrofolate reductase activityReductase domainConformational changesKinetic stepsPolypeptide chainLoop Closure and Intersubunit Communication in Tryptophan Synthase † , ‡
Schneider T, Gerhardt E, Lee M, Liang P, Anderson K, Schlichting I. Loop Closure and Intersubunit Communication in Tryptophan Synthase † , ‡. Biochemistry 1998, 37: 5394-5406. PMID: 9548921, DOI: 10.1021/bi9728957.Peer-Reviewed Original ResearchConceptsBeta-active siteMechanism of allosteric activationAlpha-active siteAlpha subunitTryptophan synthase alpha2beta2 complexPyridoxal phosphateCofactor pyridoxal phosphatePresence of serineSalmonella typhimuriumIntersubunit communicationTryptophan synthaseAllosteric activationAlpha2beta2 complexAllosteric propertiesAlpha-reactionBeta-reactionBeta subunitStructural basisAminoacrylate intermediateAminoacrylatePathwayBindingSitesTryptophanSerineLeishmania major Pteridine Reductase 1 Belongs to the Short Chain Dehydrogenase Family: Stereochemical and Kinetic Evidence †
Luba J, Nare B, Liang P, Anderson K, Beverley S, Hardy L. Leishmania major Pteridine Reductase 1 Belongs to the Short Chain Dehydrogenase Family: Stereochemical and Kinetic Evidence †. Biochemistry 1998, 37: 4093-4104. PMID: 9521731, DOI: 10.1021/bi972693a.Peer-Reviewed Original Research