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HbIDI, SlIDI and EcIDI: A comparative study of isopentenyl diphosphate isomerase activity and structure.

dc.rights.licenseopenen_US
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
dc.contributor.authorBERTHELOT, Karine
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorESTEVEZ, Yannick
dc.contributor.authorQUILIANO, Miguel
dc.contributor.authorBALDERA-AGUAYO, Pedro A
dc.contributor.authorZIMIC, Mirko
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorPRIBAT, Anne
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
dc.contributor.authorBAKLEH, Marc-Elias
hal.structure.identifierBiologie du fruit et pathologie [BFP]
hal.structure.identifierEcophysiologie et Génomique Fonctionnelle de la Vigne [UMR EGFV]
dc.contributor.authorTEYSSIER, Emeline
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorGALLUSCI, Philippe
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
dc.contributor.authorGARDRAT, Christian
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLECOMTE, Sophie
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
dc.contributor.authorPERUCH, Frédéric
dc.date.accessioned2020-03-29T10:26:25Z
dc.date.available2020-03-29T10:26:25Z
dc.date.issued2016
dc.identifier.issn0300-9084en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/4000
dc.description.abstractEnIn this study, we cloned, expressed and purified the isopentenyl diphosphate isomerases (IDIs) from two plants, Hevea brasiliensis and Solanum lycopersicum, and compared them to the already well characterized Escherichia coli IDI. Phylogenetic analysis showed high homology between the three enzymes. Their catalytic activity was investigated in vitro with recombinant purified enzymes and in vivo by complementation colorimetric tests. The three enzymes displayed consistent activities both in vitro and in vivo. In term of structure, studied by ATR-FTIR and molecular modeling, it is clear that both plant enzymes are more related to their human homologue than to E. coli IDI. But it is assumed that EcIDI represent the minimalistic part of the catalytic core, as both plant enzymes present a supplementary sequence forming an extra α-helice surrounding the catalytic site that could facilitate the biocatalysis. New potential biotechnological applications may be envisaged.
dc.language.isoENen_US
dc.subject.enAtr-Ftir
dc.subject.enEnzyme Structure-Activity
dc.subject.enHevea Brasiliensis
dc.subject.enIsopentenyl Diphosphate Isomerase
dc.subject.enIsoprenoid Biosynthesis
dc.subject.enSolanum Lycopersicum
dc.title.enHbIDI, SlIDI and EcIDI: A comparative study of isopentenyl diphosphate isomerase activity and structure.
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.biochi.2016.05.005en_US
dc.subject.halSciences du Vivant [q-bio]/Biologie végétaleen_US
bordeaux.journalBiochimieen_US
bordeaux.page133-43en_US
bordeaux.volume127en_US
bordeaux.hal.laboratoriesEcophysiologie et Génomique Fonctionnelle de la Vigne (EGFV) - UMR 1287en_US
bordeaux.institutionBordeaux Sciences Agroen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INP
bordeaux.institutionCNRS
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-02523581
hal.version1
hal.date.transferred2020-03-29T10:26:31Z
hal.exporttrue
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