1998
Substrate Channeling and Domain−Domain Interactions in Bifunctional Thymidylate Synthase−Dihydrofolate Reductase †
Liang P, Anderson K. Substrate Channeling and Domain−Domain Interactions in Bifunctional Thymidylate Synthase−Dihydrofolate Reductase †. Biochemistry 1998, 37: 12195-12205. PMID: 9724533, DOI: 10.1021/bi9803168.Peer-Reviewed Original ResearchConceptsDHFR active siteActive siteTS active siteCrystal structureTransient kinetic analysisEnzyme active siteBifunctional TS-DHFRProtein surfaceTS-DHFRKinetics of substrateReductase enzymeSingle polypeptide chainKinetic analysisDihydrofolateThymidylate synthasePolypeptide chainSubstrateEnzymeStructureDomain-domain interactionsSpecies of protozoaInteractionKineticsL. majorChainLoop Closure and Intersubunit Communication in Tryptophan Synthase † , ‡
Schneider T, Gerhardt E, Lee M, Liang P, Anderson K, Schlichting I. Loop Closure and Intersubunit Communication in Tryptophan Synthase † , ‡. Biochemistry 1998, 37: 5394-5406. PMID: 9548921, DOI: 10.1021/bi9728957.Peer-Reviewed Original ResearchConceptsBeta-active siteMechanism of allosteric activationAlpha-active siteAlpha subunitTryptophan synthase alpha2beta2 complexPyridoxal phosphateCofactor pyridoxal phosphatePresence of serineSalmonella typhimuriumIntersubunit communicationTryptophan synthaseAllosteric activationAlpha2beta2 complexAllosteric propertiesAlpha-reactionBeta-reactionBeta subunitStructural basisAminoacrylate intermediateAminoacrylatePathwayBindingSitesTryptophanSerine
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