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Article

A redox-active isopropylmalate dehydrogenase functions in the biosynthesis of glucosinolates and leucine in Arabidopsis.

The Plant journal : for cell and molecular biology - 1 Nov 2009

He Yan, Mawhinney Thomas P, Preuss Mary L, Schroeder Amy C, Chen Bing, Abraham Linda, Jez Joseph M, Chen Sixue

Abstract excerpt

We report a detailed functional characterization of an Arabidopsis isopropylmalate dehydrogenase (AtIPMDH1) that is involved in both glucosinolate biosynthesis and leucine biosynthesis. AtIPMDH1 shares high homology with enzymes from bacteria and yeast that are known to function in leucine biosynthesis. In plants, AtIPMDH1 is co-expressed with nearly all the genes known to be involved in aliphatic glucosinolate...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Enzymologic

Share to Glucosinolates

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Share to Malate Dehydrogenase

Share to Mutagenesis, Insertional

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Source

Identifiers

PMID: 19674406
DOI: 10.1111/j.1365-313X.2009.03990.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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