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

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...

Full description

Saved in:
Bibliographic Details
Published in:Journal of plant physiology 2021-02, Vol.257, p.153350-153350, Article 153350
Main Authors: Eprintsev, Alexander T., Fedorin, Dmitry N., Dobychina, Maria A., Igamberdiev, Abir U.
Format: Article
Language:English
Subjects:
Aconitate isomerase
Aconitic acid
Citrate
Citric acid
Corn
Enzymes
Gene expression
Isomers
Maize (Zea mays L.)
Malate
Photosynthesis
Phytochrome
Substrates
Trans-aconitate
Tricarboxylic acid cycle
Zea mays
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0176-1617
1618-1328
DOI:10.1016/j.jplph.2020.153350