Literature DB >> 3049163

The herbicidally active experimental compound Hoe 704 is a potent inhibitor of the enzyme acetolactate reductoisomerase.

A Schulz1, P Spönemann, H Köcher, F Wengenmayer.   

Abstract

Growth inhibition of plants and bacteria by the experimental herbicide Hoe 704 (2-methylphosphinoyl-2-hydroxyacetic acid) was alleviated by the addition of the branched-chain amino acids to growth media. Hoe 704 caused a massive accumulation of acetoin and acetolactate, indicating its direct interference with the branched-chain amino acid biosynthetic pathway. The second enzyme of this pathway, acetolactate reductoisomerase (EC 1.1.1.86), was found to be subject to strong inhibition by Hoe 704. The inhibition was time-dependent and competitive with the enzyme's substrate, acetolactate. This report establishes acetolactate reductoisomerase as a new target for a herbicidal compound.

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Year:  1988        PMID: 3049163     DOI: 10.1016/0014-5793(88)80515-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  11 in total

1.  Molecular regulation of amino acid biosynthesis in plants.

Authors:  B K Singh; B F Matthews
Journal:  Amino Acids       Date:  1994-06       Impact factor: 3.520

Review 2.  Targeting Metalloenzymes for Therapeutic Intervention.

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Journal:  Chem Rev       Date:  2018-09-07       Impact factor: 60.622

3.  Synthesis, structure, and biological activity of novel (oxdi/tri)azoles derivatives containing 1,2,3-thiadiazole or methyl moiety.

Authors:  Xing-Hai Liu; Li Pan; Jian-Quan Weng; Cheng-Xia Tan; Yong-Hong Li; Bao-Lei Wang; Zheng-Ming Li
Journal:  Mol Divers       Date:  2012-01-17       Impact factor: 2.943

4.  The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution.

Authors:  V Biou; R Dumas; C Cohen-Addad; R Douce; D Job; E Pebay-Peyroula
Journal:  EMBO J       Date:  1997-06-16       Impact factor: 11.598

5.  Isolation, characterization and sequence analysis of a full-length cDNA clone encoding acetohydroxy acid reductoisomerase from spinach chloroplasts.

Authors:  R Dumas; M Lebrun; R Douce
Journal:  Biochem J       Date:  1991-07-15       Impact factor: 3.857

6.  Isolation and kinetic properties of acetohydroxy acid isomeroreductase from spinach (Spinacia oleracea) chloroplasts overexpressed in Escherichia coli.

Authors:  R Dumas; D Job; J Y Ortholand; G Emeric; A Greiner; R Douce
Journal:  Biochem J       Date:  1992-12-15       Impact factor: 3.857

7.  Interactions of plant acetohydroxy acid isomeroreductase with reaction intermediate analogues: correlation of the slow, competitive, inhibition kinetics of enzyme activity and herbicidal effects.

Authors:  R Dumas; C Cornillon-Bertrand; P Guigue-Talet; P Genix; R Douce; D Job
Journal:  Biochem J       Date:  1994-08-01       Impact factor: 3.857

8.  Metabolic effects of inhibitors of two enzymes of the branched-chain amino acid pathway in Salmonella typhimurium.

Authors:  S Epelbaum; D M Chipman; Z Barak
Journal:  J Bacteriol       Date:  1996-02       Impact factor: 3.490

9.  Nucleotide sequence and characterization of a cDNA encoding the acetohydroxy acid isomeroreductase from Arabidopsis thaliana.

Authors:  G Curien; R Dumas; R Douce
Journal:  Plant Mol Biol       Date:  1993-02       Impact factor: 4.076

10.  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).

Authors:  R Dumas; G Curien; R T DeRose; R Douce
Journal:  Biochem J       Date:  1993-09-15       Impact factor: 3.857

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