Threonine-509 Is a Determinant of Apparent Affinity for Both Substrate and Cations in the Human Na+/Dicarboxylate Cotransporter †
Weerachayaphorn J, Pajor AM. Threonine-509 Is a Determinant of Apparent Affinity for Both Substrate and Cations in the Human Na+/Dicarboxylate Cotransporter †. Biochemistry 2007, 47: 1087-1093. PMID: 18161988, PMCID: PMC2570185, DOI: 10.1021/bi701417h.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAnimalsChlorocebus aethiopsCitric AcidCOS CellsDicarboxylic Acid TransportersGene ExpressionHumansKineticsMolecular Sequence DataMutationOrganic Anion Transporters, Sodium-DependentRabbitsRecombinant ProteinsSequence Homology, Amino AcidSodiumSubstrate SpecificitySuccinic AcidSymportersThreonineConceptsTransmembrane helix 7Functional differencesApparent affinityApparent sodium affinitySubstrate Binding SiteAmino acid differencesCitric acid cycleCitrate affinityHelix 7Substrate specificityPosition -509Rabbit sequenceIndividual residuesAcid cycleAcid differencesSimilar apparent affinitiesLoop regionIntermediate KmAmino acidsBinding sitesMutantsNaDC1SerineThreonineExhibit differencesIdentification of transport pathways for citric acid cycle intermediates in the human colon carcinoma cell line, Caco-2
Weerachayaphorn J, Pajor AM. Identification of transport pathways for citric acid cycle intermediates in the human colon carcinoma cell line, Caco-2. Biochimica Et Biophysica Acta 2007, 1778: 1051-1059. PMID: 18194662, PMCID: PMC2323910, DOI: 10.1016/j.bbamem.2007.12.013.Peer-Reviewed Original ResearchBiological TransportCaco-2 CellsCitratesCitric Acid CycleColonic NeoplasmsDicarboxylic Acid TransportersEpithelial CellsExtracellular SpaceGene Expression RegulationHumansIntracellular SpaceKineticsModels, BiologicalOrganic Anion TransportersOrganic Anion Transporters, Sodium-DependentPlasticsReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSodiumSubstrate SpecificitySuccinatesSymportersTime FactorsTransfectionSodium-dependent Extracellular Accessibility of Lys-84 in the Sodium/Dicarboxylate Cotransporter*
Weerachayaphorn J, Pajor AM. Sodium-dependent Extracellular Accessibility of Lys-84 in the Sodium/Dicarboxylate Cotransporter*. Journal Of Biological Chemistry 2007, 282: 20213-20220. PMID: 17504760, PMCID: PMC2864014, DOI: 10.1074/jbc.m701113200.Peer-Reviewed Original ResearchConceptsLys-84Transmembrane helicesMTS inhibitionLarge-scale conformational changesTranslocation of substratesCysteine-specific reagentsTransmembrane helix 3SLC13 familyCitric acid cycle intermediatesExtracellular halfEpithelial cell lineExtracellular accessibilityHelix 3Transport cycleTrp-103Human retinal pigment epithelial cell lineAddition of substrateConformational changesLeu-111Conformational statesRetinal pigment epithelial cell lineSubstrate affinityReentrant loopAmino acidsGlu-101