2002
Mechanistic Characterization of Toxoplasma gondiiThymidylate Synthase (TS-DHFR)-Dihydrofolate Reductase EVIDENCE FOR A TS INTERMEDIATE AND TS HALF-SITES REACTIVITY*
Johnson E, Hinz W, Atreya C, Maley F, Anderson K. Mechanistic Characterization of Toxoplasma gondiiThymidylate Synthase (TS-DHFR)-Dihydrofolate Reductase EVIDENCE FOR A TS INTERMEDIATE AND TS HALF-SITES REACTIVITY*. Journal Of Biological Chemistry 2002, 277: 43126-43136. PMID: 12192007, DOI: 10.1074/jbc.m206523200.Peer-Reviewed Original ResearchThe Kinetic Mechanism of the Human Bifunctional Enzyme ATIC (5-Amino-4-imidazolecarboxamide Ribonucleotide Transformylase/Inosine 5′-Monophosphate Cyclohydrolase) A SURPRISING LACK OF SUBSTRATE CHANNELING*
Bulock K, Beardsley G, Anderson K. The Kinetic Mechanism of the Human Bifunctional Enzyme ATIC (5-Amino-4-imidazolecarboxamide Ribonucleotide Transformylase/Inosine 5′-Monophosphate Cyclohydrolase) A SURPRISING LACK OF SUBSTRATE CHANNELING*. Journal Of Biological Chemistry 2002, 277: 22168-22174. PMID: 11948179, DOI: 10.1074/jbc.m111964200.Peer-Reviewed Original ResearchConceptsCyclohydrolase reactionProduction of inosine monophosphateRelease of tetrahydrofolateSteady-state kinetic techniquesStopped-flow absorbanceBifunctional enzymeActive siteBifunctional proteinSubstrate channelingInosine 5'-monophosphateCyclohydrolaseEnzymatic activityChemotherapeutic targetEnzyme reaction pathwayInosine monophosphateKinetic mechanismFormyltransferaseProteinEnzymeKinetic analysisPathwayKinetic advantageKinetic evidenceKinetic techniquesRibonucleotides
2001
Y265H Mutator Mutant of DNA Polymerase β PROPER GEOMETRIC ALIGNMENT IS CRITICAL FOR FIDELITY*
Shah A, Li S, Anderson K, Sweasy J. Y265H Mutator Mutant of DNA Polymerase β PROPER GEOMETRIC ALIGNMENT IS CRITICAL FOR FIDELITY*. Journal Of Biological Chemistry 2001, 276: 10824-10831. PMID: 11154692, DOI: 10.1074/jbc.m008680200.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsDNA Polymerase betaMutationProtein ConformationStructure-Activity RelationshipConceptsDNA polymerase betaPolymerase betaVivo genetic screenWild-type proteinWild-type enzymeActive site residuesGenetic screenTyr-265Mutant proteinsMutator mutantsPolymerase structureProper geometric alignmentSite residuesProtein conformationNucleotidyl transferForward mutationDNA polymerasePolymerase fidelityDNTP substratesDNA synthesisProteinDeoxynucleoside triphosphatesFirst evidenceTemplate A.Enzyme
1999
[6] Fundamental mechanisms of substrate channeling
Anderson K. [6] Fundamental mechanisms of substrate channeling. Methods In Enzymology 1999, 308: 111-145. PMID: 10507003, DOI: 10.1016/s0076-6879(99)08008-8.Peer-Reviewed Original ResearchAnimalsBinding SitesCarbamoyl-Phosphate Synthase (Ammonia)Citrate (si)-SynthaseDiffusionDimerizationGlycerophosphatesIndolesKineticsLeishmania majorMagnetic Resonance SpectroscopyMalate DehydrogenaseModels, MolecularMultienzyme ComplexesMutationPeptide SynthasesProtein ConformationSalmonella typhimuriumTetrahydrofolate DehydrogenaseThymidylate SynthaseTryptophan Synthase
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 chainStructure and Functional Relationships in Human pur H
Beardsley G, Rayl E, Gunn K, Moroson B, Seow H, Anderson K, Vergis J, Fleming K, Worland S, Condon B, Davies J. Structure and Functional Relationships in Human pur H. Advances In Experimental Medicine And Biology 1998, 431: 221-226. PMID: 9598063, DOI: 10.1007/978-1-4615-5381-6_43.Peer-Reviewed Original Research
1997
Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude
Munson M, Anderson K, Regan L. Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude. Structure 1997, 2: 77-87. PMID: 9080201, DOI: 10.1016/s1359-0278(97)00008-4.Peer-Reviewed Original Research
1996
Surface point mutations that significantly alter the structure and stability of a protein's denatured state
Smith C, Bu Z, Engelman D, Regan L, Anderson K, Sturtevant J. Surface point mutations that significantly alter the structure and stability of a protein's denatured state. Protein Science 1996, 5: 2009-2019. PMID: 8897601, PMCID: PMC2143264, DOI: 10.1002/pro.5560051007.Peer-Reviewed Original ResearchConceptsPoint mutationsDenatured stateStopped-flow fluorescenceDenaturant concentrationSolvent-exposed sitesStreptococcal protein GMutantsG mutantTertiary structureGuHCl denaturationEquilibrium intermediatesPosition 53B1 domainProteinCircular dichroismMutationsProtein GGuanidine hydrochlorideSmall-angle X-ray scatteringStructural implicationsX-ray scatteringFluorescenceThrRadius of gyrationDenaturantsIntersubunit Communication in Tryptophan Synthase by Carbon-13 and Fluorine-19 REDOR NMR †
McDowell L, Lee M, McKay R, Anderson K, Schaefer J. Intersubunit Communication in Tryptophan Synthase by Carbon-13 and Fluorine-19 REDOR NMR †. Biochemistry 1996, 35: 3328-3334. PMID: 8605170, DOI: 10.1021/bi9518297.Peer-Reviewed Original ResearchConceptsProton dipolar decouplingMagic angle spinningLocal electric field gradientsElectric field gradientIsotropic shiftsLigand bindingChemical shiftsNMR spectraConformational gatingEnzyme tryptophan synthaseBeta subunitCarbon-13Dipolar decouplingTryptophan synthaseMother liquorResolved linesConformational rearrangementsBinding of serineNMRLigandField gradientEnzyme complexIntersubunit communicationTyrosine residuesSubunit
1995
Kinetic Characterization of Channel Impaired Mutants of Tryptophan Synthase (∗)
Anderson K, Kim A, Quillen J, Sayers E, Yang X, Miles E. Kinetic Characterization of Channel Impaired Mutants of Tryptophan Synthase (∗). Journal Of Biological Chemistry 1995, 270: 29936-29944. PMID: 8530393, DOI: 10.1074/jbc.270.50.29936.Peer-Reviewed Original ResearchBinding SitesCarbon RadioisotopesGlycerophosphatesIndolesKineticsMacromolecular SubstancesMathematicsModels, TheoreticalMutagenesis, Site-DirectedPoint MutationProtein ConformationRadioisotope Dilution TechniqueRecombinant ProteinsSalmonella typhimuriumSerineStructure-Activity RelationshipTryptophan SynthaseMechanism of Inhibition of HIV-1 Reverse Transcriptase by Nonnucleoside Inhibitors
Spence R, Kati W, Anderson K, Johnson K. Mechanism of Inhibition of HIV-1 Reverse Transcriptase by Nonnucleoside Inhibitors. Science 1995, 267: 988-993. PMID: 7532321, PMCID: PMC7526747, DOI: 10.1126/science.7532321.Peer-Reviewed Original ResearchConceptsActive site catalytic residuesPre-steady-state kinetic analysisNucleotide-induced conformational changesInterfere with nucleotide bindingPre-steady-state burstEnzyme-DNA complexPre-steady-stateReverse transcriptasePresence of saturating concentrationsCatalytic residuesNucleotide bindingNucleoside triphosphatesDNA polymerizationNucleotide analogsHydrophobic pocketMechanism of inhibitionNonnucleoside inhibitorsConformational changesNoncompetitive inhibitorInhibition of HIV-1 reverse transcriptaseKinetic analysisHIV-1 reverse transcriptaseSaturating concentrationsTranscriptaseInhibitors
1991
Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism
Anderson K, Miles E, Johnson K. Serine modulates substrate channeling in tryptophan synthase. A novel intersubunit triggering mechanism. Journal Of Biological Chemistry 1991, 266: 8020-8033. PMID: 1902468, DOI: 10.1016/s0021-9258(18)92934-0.Peer-Reviewed Original ResearchConceptsIndole-3-glycerol phosphateTryptophan synthaseProtein conformationAlpha 2 beta 2 complexReaction of serineAbsence of serineBeta siteFormation of tryptophanAlpha siteSteady-state turnoverActive siteAccumulation of indoleAlpha reactionSubstitution of cysteineSubstrate channelingBeta reactionBeta subunitMetabolic intermediatesSerineAlpha subunitQuench-flowProtein fluorescenceTurnover experimentsProteinTryptophan release