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
1993
EPSP synthase inhibitor design II. The importance of the 3-phosphate group for ligand binding at the shikimate-3-phosphate site & the identification of 3-malonate ethers as novel 3-phosphate mimics.
Miller M, Anderson K, Braccolino D, Cleary D, Gruys K, Han C, Lin K, Pansegrau P, Ream J, Sammons R, Sikorski J. EPSP synthase inhibitor design II. The importance of the 3-phosphate group for ligand binding at the shikimate-3-phosphate site & the identification of 3-malonate ethers as novel 3-phosphate mimics. Bioorganic & Medicinal Chemistry Letters 1993, 3: 1435-1440. DOI: 10.1016/s0960-894x(01)80425-x.Peer-Reviewed Original Research
1991
Synthesis and evaluation of two new inhibitors of EPSP synthase
Pansegrau P, Anderson K, Widlanski T, Ream J, Sammons R, Sikorski J, Knowles J. Synthesis and evaluation of two new inhibitors of EPSP synthase. Tetrahedron Letters 1991, 32: 2589-2592. DOI: 10.1016/s0040-4039(00)78792-2.Peer-Reviewed Original Research
1990
"Kinetic competence" of the 5-enolpyruvoylshikimate-3-phosphate synthase tetrahedral intermediate.
Anderson K, Johnson K. "Kinetic competence" of the 5-enolpyruvoylshikimate-3-phosphate synthase tetrahedral intermediate. Journal Of Biological Chemistry 1990, 265: 5567-5572. PMID: 2180929, DOI: 10.1016/s0021-9258(19)39398-6.Peer-Reviewed Original Research
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 phosphateEvaluation of 5-enolpyruvoylshikimate-3-phosphate synthase substrate and inhibitor binding by stopped-flow and equilibrium fluorescence measurements.
Anderson K, Sikorski J, Johnson K. Evaluation of 5-enolpyruvoylshikimate-3-phosphate synthase substrate and inhibitor binding by stopped-flow and equilibrium fluorescence measurements. Biochemistry 1988, 27: 1604-10. PMID: 3284585, DOI: 10.1021/bi00405a032.Peer-Reviewed Original ResearchConceptsBinding of substratesBinary complexShikimate 3-phosphateStopped-flow fluorescence methodsDissociation constantFree enzymeGlyphosate bindingS3P bindingInhibitor bindingProtein fluorescenceKinetics of bindingTernary complexEnzymeStopped-flowFluorescence measurementsBindingFluorescence titrationSaturating concentrationsS3PEquilibrium fluorescence measurements