1999
The Catalytic Mechanism of EPSP Synthase Revisited †
Lewis J, Johnson K, Anderson K. The Catalytic Mechanism of EPSP Synthase Revisited †. Biochemistry 1999, 38: 7372-7379. PMID: 10353849, DOI: 10.1021/bi9830258.Peer-Reviewed Original ResearchMeSH Keywords3-Phosphoshikimate 1-CarboxyvinyltransferaseAlkyl and Aryl TransferasesAmino Acid SubstitutionBinding SitesCatalysisChromatography, High Pressure LiquidEscherichia coliFreezingKineticsMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularPhosphoenolpyruvateProtonsSubstrate SpecificityConceptsEPSP synthaseEnzyme intermediateKinetic competenceSingle-turnover experimentsSubstrate to productSolid-state NMRSolid-state NMR studiesEnzyme assaysEnzyme reaction pathwaySDS-PAGECatalytic mechanismDegrees CSpeciesEnzymeIntermediate speciesNMR studiesSide productsCharacterized reaction productsSample preparationDisappearance of substrateSynthaseReaction productsFormation of productsBreakdown productsReaction pathways
1997
Pre-Steady-State Kinetic Analysis of the Trichodiene Synthase Reaction Pathway †
Cane D, Chiu H, Liang P, Anderson K. Pre-Steady-State Kinetic Analysis of the Trichodiene Synthase Reaction Pathway †. Biochemistry 1997, 36: 8332-8339. PMID: 9204880, DOI: 10.1021/bi963018o.Peer-Reviewed Original ResearchConceptsChemical catalysisReaction pathwaysRapid chemical quench methodsActive siteSteady-state catalytic rateSingle turnover reactionsRate constant kcatEnzyme active siteNerolidyl diphosphateDeuterium isotope effectSingle-turnover experimentsSingle turnover rateState kinetic analysisTurnover reactionsDetection limitCatalytic rateOverall reactionSteady-state releaseIsotope effectRate-limiting stepState kineticsCatalysisReactionQuench methodSynthase reaction