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
1996
Intersubunit 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
Expression of Human Cyclophilin‐40 and the Effect of the His141→Trp Mutation on Catalysis and Cyclosporin A Binding
Hoffmann K, Kakalis L, Anderson K, Armitage I, Handschumacher R. Expression of Human Cyclophilin‐40 and the Effect of the His141→Trp Mutation on Catalysis and Cyclosporin A Binding. The FEBS Journal 1995, 229: 188-193. PMID: 7744028, DOI: 10.1111/j.1432-1033.1995.0188l.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid IsomerasesBase SequenceBinding SitesCarrier ProteinsCyclophilin DCyclophilinsCyclosporineEnzyme ActivationEscherichia coliHumansMagnetic Resonance SpectroscopyModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPeptidylprolyl IsomeraseProtein BindingRecombinant ProteinsConceptsCyP-40Isomerase activityPeptidyl-prolyl cis-trans isomerase activityHuman cyclophilin-40PGEX-3X expression vectorSite-directed mutagenesisMutant proteinsCyclophilin 40Intrinsic isomerase activityNMR difference spectroscopySuccinyl-AlaExpression vectorHistidine residuesEscherichia coliTryptophan residuesProteinCyclophilinMolecular modellingAla-ProResiduesGel filtrationWeak affinityBindingHigh affinityAffinity matrix
1994
Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ.
Brown E, Marquardt J, Lee J, Walsh C, Anderson K. Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ. Biochemistry 1994, 33: 10638-45. PMID: 8075064, DOI: 10.1021/bi00201a010.Peer-Reviewed Original ResearchMeSH KeywordsAlkyl and Aryl TransferasesBacterial ProteinsBinding SitesCatalysisEscherichia coliKineticsMagnetic Resonance SpectroscopyPhosphoenolpyruvateTransferasesConceptsUDP-N-acetylglucosamineUDP-GlcNAcAbsence of UDP-GlcNAcChemical quench analysisPresence of UDP-GlcNAcSingle-turnover conditionsBinding constantsPeptidoglycan biosynthesisSolution NMRC-2Enzyme nucleophilePeptide of molecular weightStoichiometric labelingConsistent with catalysisRemoval of small moleculesE. coliAdductsSmall moleculesMurZEnzyme adductNon-covalentlySDS-PAGEM ureaLabeled peptidesEnzyme
1990
Observation by 13C NMR of the EPSP synthase tetrahedral intermediate bound to the enzyme active site.
Anderson K, Sammons R, Leo G, Sikorski J, Benesi A, Johnson K. Observation by 13C NMR of the EPSP synthase tetrahedral intermediate bound to the enzyme active site. Biochemistry 1990, 29: 1460-5. PMID: 2334707, DOI: 10.1021/bi00458a017.Peer-Reviewed Original ResearchConceptsEnzyme active siteTetrahedral intermediateFormation of pyruvateActive siteEnzyme sitesComparison of quenchingReaction of enzymeTime of incubationTetrahedral centerCompound giving riseReaction pathwaysEnzymatic hydrolysisPeak assignmentsEnzymeNMR experimentsTernary complexNMR measurementsSide productsRate of formationSpectroscopic probesLong time of incubationNMRSpeciesTriethylamineCovalent adducts