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Nucleotide sequence and characterization of a cDNA encoding the acetohydroxy acid isomeroreductase from Arabidopsis thaliana.
Unité Mixte CNRS/Rhône-Poulenc Agrochimie, Lyon, France.
The primary structure of acetohydroxy acid isomeroreductase from Arabidopsis thaliana was deduced from two overlapping cDNA. The full-length cDNA sequence predicts an amino acid sequence for the protein precursor of 591 residues including a putative transit peptide of 67 amino acids. Comparison of the A. thaliana and spinach acetohydroxy acid isomeroreductases reveals that the sequences are conserved in the mature protein regions, but divergent in the transit peptides and around their putative processing site.
PMID: 8448371 [PubMed - indexed for MEDLINE]
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Cited by 2 PubMed Central articles
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Branched-chain-amino-acid biosynthesis in plants: molecular cloning and characterization of the gene encoding acetohydroxy acid isomeroreductase (ketol-acid reductoisomerase) from Arabidopsis thaliana (thale cress).
Dumas R, Curien G, DeRose RT, Douce R.
Biochem J. 1993 Sep 15; 294 ( Pt 3):821-8.
[Biochem J. 1993]
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Interactions of plant acetohydroxy acid isomeroreductase with reaction intermediate analogues: correlation of the slow, competitive, inhibition kinetics of enzyme activity and herbicidal effects.
Dumas R, Cornillon-Bertrand C, Guigue-Talet P, Genix P, Douce R, Job D.
Biochem J. 1994 Aug 1; 301 ( Pt 3):813-20.
[Biochem J. 1994]