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

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dc.contributor.author Berthelot, Karine
dc.contributor.author Estevez, Yannick
dc.contributor.author Quiliano, Miguel
dc.contributor.author Baldera-Aguayo, Pedro-A.
dc.contributor.author Zimic-Peralta, Mirko Juan
dc.contributor.author Pribat, Anne
dc.contributor.author Bakleh, Marc-Elias
dc.contributor.author Teyssier, Emeline
dc.contributor.author Gallusci, Philippe
dc.contributor.author Gardrat, Christian
dc.contributor.author Lecomte, Sophie
dc.contributor.author Peruch, Frederic
dc.date.accessioned 2019-02-06T14:45:11Z
dc.date.available 2019-02-06T14:45:11Z
dc.date.issued 2016
dc.identifier.uri https://hdl.handle.net/20.500.12866/5031
dc.description.abstract In 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. en_US
dc.language.iso eng
dc.publisher Elsevier
dc.relation.ispartofseries Biochimie
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
dc.subject Amino Acid Sequence en_US
dc.subject ATR-FTIR en_US
dc.subject Biocatalysis en_US
dc.subject Carbon-Carbon Double Bond Isomerases/chemistry/metabolism en_US
dc.subject Enzyme structure-activity en_US
dc.subject Escherichia coli/enzymology en_US
dc.subject Hevea brasiliensis en_US
dc.subject Hevea/enzymology en_US
dc.subject Humans en_US
dc.subject Isopentenyl diphosphate isomerase en_US
dc.subject Isoprenoid biosynthesis en_US
dc.subject Lycopersicon esculentum/enzymology en_US
dc.subject Models, Molecular en_US
dc.subject Solanum lycopersicum en_US
dc.subject Species Specificity en_US
dc.title HbIDI, SlIDI and EcIDI: A comparative study of isopentenyl diphosphate isomerase activity and structure en_US
dc.type info:eu-repo/semantics/article
dc.identifier.doi https://doi.org/10.1016/j.biochi.2016.05.005
dc.subject.ocde https://purl.org/pe-repo/ocde/ford#1.06.03
dc.relation.issn 1638-6183

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