2017
Understanding the molecular mechanism of substrate channeling and domain communication in protozoal bifunctional TS-DHFR
Anderson K. Understanding the molecular mechanism of substrate channeling and domain communication in protozoal bifunctional TS-DHFR. Protein Engineering Design And Selection 2017, 30: 253-261. PMID: 28338744, PMCID: PMC6438133, DOI: 10.1093/protein/gzx004.Peer-Reviewed Original ResearchConceptsBifunctional thymidylate synthase-dihydrofolate reductaseThymidylate synthase-dihydrofolate reductaseSubstrate channelingDihydrofolate reductaseN-terminal amino acid extensionAmino acid extensionDihydrofolate reductase domainThymidylate synthaseFolate metabolizing enzymesAcid extensionMonofunctional formsPolypeptide chainMutation analysisMolecular mechanismsMetabolic enzymesParasitic protozoaDNA synthesisFunctional regionsInhibitor designSpeciesEnzymeStructural similarityStructural studiesEfficient catalysisLeishmania major
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 chain