Mostrar el registro sencillo del ítem

Characterization of l-aspartate oxidase from <em>Arabidopsis thaliana.</em>

hal.structure.identifierInstitut des Sciences des Plantes de Paris-Saclay [IPS2 (UMR_9213 / UMR_1403)]
dc.contributor.authorHAO, Jingfang
hal.structure.identifierBiologie du fruit et pathologie [BFP]
hal.structure.identifierInstitut des Sciences des Plantes de Paris-Saclay [IPS2 (UMR_9213 / UMR_1403)]
dc.contributor.authorPÉTRIACQ, Pierre
hal.structure.identifierInstitut des Sciences des Plantes de Paris-Saclay [IPS2 (UMR_9213 / UMR_1403)]
dc.contributor.authorDE BONT, Linda
hal.structure.identifierInstitut des Sciences des Plantes de Paris-Saclay [IPS2 (UMR_9213 / UMR_1403)]
dc.contributor.authorHODGES, Michael
hal.structure.identifierInstitut des Sciences des Plantes de Paris-Saclay [IPS2 (UMR_9213 / UMR_1403)]
dc.contributor.authorGAKIÈRE, Bertrand
dc.date.issued2018
dc.identifier.issn0168-9452
dc.description.abstractEnThe flavoprotein l-aspartate oxidase (LASPO) is the first enzyme of the de novo biosynthetic pathway of NAD+ in plants. Although LASPO is considered pivotal to maintain NAD+ homeostasis, it has not been hitherto characterized in plants. Here, the cDNA encoding the LASPO from the model plant Arabidopsis thaliana (AtLASPO, At5g14760) has been cloned and expressed in Escherichia coli for subsequent enzyme characterization. The purified AtLASPO enzyme displayed a Km of 0.79 mM for l-aspartate and a kcat of 0.25 s−1. We could further detect an l-aspartate: fumarate oxidoreductase activity of the recombinant plant enzyme. In addition, results indicated that NADP+ but not NAD+, and even more strongly NADH, inhibited AtLASPO at physiological concentrations by competing with the flavin for binding to the apoprotein. LASPO optimal pH and temperature, as well as plastidial pyridine nucleotide concentrations may contribute to an increased NAD+ production in planta. Moreover, in Arabidopsis thaliana AtLASPO gene expression exhibited a clear correlation between LASPO activity and NAD+ levels, thus demonstrating that plant LASPO catalyzes a key metabolic step of NAD+ synthesis.
dc.description.sponsorshipSaclay Plant Sciences - ANR-10-LABX-0040
dc.description.sponsorshipIdex Paris-Saclay - ANR-11-IDEX-0003
dc.language.isoen
dc.publisherElsevier
dc.subjectRegulation
dc.subject.enArabidopsis thaliana
dc.subject.enCompetitive inhibition
dc.subject.enNAD(+) biosynthesis
dc.subject.enl-aspartate oxidase
dc.title.enCharacterization of l-aspartate oxidase from <em>Arabidopsis thaliana.</em>
dc.typeArticle de revue
dc.identifier.doi10.1016/j.plantsci.2018.03.016
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale
bordeaux.journalPlant Science
bordeaux.page133-142
bordeaux.volume271
bordeaux.peerReviewedoui
hal.identifierhal-02621906
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02621906v1
bordeaux.COinSctx_ver=Z39.88-2004&amp;rft_val_fmt=info:ofi/fmt:kev:mtx:journal&amp;rft.jtitle=Plant%20Science&amp;rft.date=2018&amp;rft.volume=271&amp;rft.spage=133-142&amp;rft.epage=133-142&amp;rft.eissn=0168-9452&amp;rft.issn=0168-9452&amp;rft.au=HAO,%20Jingfang&amp;P%C3%89TRIACQ,%20Pierre&amp;DE%20BONT,%20Linda&amp;HODGES,%20Michael&amp;GAKI%C3%88RE,%20Bertrand&amp;rft.genre=article


Archivos en el ítem

ArchivosTamañoFormatoVer

No hay archivos asociados a este ítem.

Este ítem aparece en la(s) siguiente(s) colección(ones)

Mostrar el registro sencillo del ítem