Aconitate isomerase from maize leaves : Light-dependent expression and kinetic properties

Copyright © 2020 Elsevier GmbH. All rights reserved.

Détails bibliographiques
Publié dans:Journal of plant physiology. - 1979. - 257(2021) vom: 15. Feb., Seite 153350
Auteur principal: Eprintsev, Alexander T (Auteur)
Autres auteurs: Fedorin, Dmitry N, Dobychina, Maria A, Igamberdiev, Abir U
Format: Article en ligne
Langue:English
Publié: 2021
Accès à la collection:Journal of plant physiology
Sujets:Journal Article Aconitate isomerase Citrate Maize (Zea mays L.) Phytochrome Trans-aconitate Plant Proteins Aconitic Acid 93371T1BXP Isomerases EC 5.-
Description
Résumé:Copyright © 2020 Elsevier GmbH. All rights reserved.
Aconitate isomerase (EC 5.3.3.7) interconverts cis- and trans-isomers of aconitic acid. Expression of the gene encoding this enzyme was studied in maize (Zea mays L.) leaves depending on light regime. Aconitate isomerase was induced by white and by red light indicating the involvement of phytochrome in the regulation of gene expression. The enzyme was partially purified from maize leaves. The value of Km was 0.75 mM with cis-aconitate and 0.92 mM with trans-aconitate, pH optimum was 8.0-8.2 with both substrates, citrate and malate suppressed its activity. It is concluded that aconitate isomerase actively participates in the interconversion of cis- and trans-aconitate in the light providing a possibility of using the pool of trans-aconitate for the regulation of the tricarboxylic acid cycle activity and mediating citrate/isocitrate supply for the biosynthetic and signaling purposes in photosynthetic cells
Description:Date Completed 27.05.2021
Date Revised 27.05.2021
published: Print-Electronic
Citation Status MEDLINE
ISSN:1618-1328
DOI:10.1016/j.jplph.2020.153350