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
1988
A tetrahedral intermediate in the EPSP synthase reaction observed by rapid quench kinetics.
Anderson K, Sikorski J, Johnson K. A tetrahedral intermediate in the EPSP synthase reaction observed by rapid quench kinetics. Biochemistry 1988, 27: 7395-406. PMID: 3061457, DOI: 10.1021/bi00419a034.Peer-Reviewed Original ResearchConceptsPhosphoenol pyruvateBurst of product formationPre-steady-state burstQuantitation of reaction productsTransient-state kinetic analysisEnzyme-bound intermediateShikimate 3-phosphateSingle turnover experimentsPre-steady-stateSubstrate trapping experimentsRelease of substratesEquilibrium constantsSynthase reactionExcess enzymeBinding rateAbsence of phosphatePyruvateReverse reactionEnzymeTurnover experimentsEnzymatic reactionsKinetic competenceEnzyme concentrationFormation of productsConcentration of phosphate