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
1995
Reevaluating glyphosate as a transition-state inhibitor of EPSP synthase: identification of an EPSP synthase.EPSP.glyphosate ternary complex.
Sammons R, Gruys K, Anderson K, Johnson K, Sikorski J. Reevaluating glyphosate as a transition-state inhibitor of EPSP synthase: identification of an EPSP synthase.EPSP.glyphosate ternary complex. Biochemistry 1995, 34: 6433-40. PMID: 7756274, DOI: 10.1021/bi00019a024.Peer-Reviewed Original ResearchConceptsEPSP synthaseTernary complexShikimate 3-phosphateSteady-state kineticsEnzyme active siteTransition-state analogSubstrate turnoverSynthase reactionTransition-state inhibitorsEnzymeAssociated with PEPUncompetitive inhibitorBinding resultsSynthaseActive siteFluorescence titration experimentsShikimateOxonium ionsTurnoverInteraction of glyphosateTitration experiments
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