Fermentative Metabolism Is Induced by Inhibiting Different Enzymes of the Branched-Chain Amino Acid Biosynthesis Pathway in Pea Plants

2005 ◽  
Vol 53 (19) ◽  
pp. 7486-7493 ◽  
Author(s):  
Ana Zabalza ◽  
Esther M. González ◽  
Cesar Arrese-Igor ◽  
Mercedes Royuela
Keyword(s):  
Amino Acid ◽  
Amino Acid Biosynthesis ◽  
Biosynthesis Pathway ◽  
Acid Biosynthesis ◽  
Fermentative Metabolism ◽  
Branched Chain Amino Acid ◽  
Branched Chain

scholarly journals Auxotrophy Accounts for Nodulation Defect of Most Sinorhizobium meliloti Mutants in the Branched-Chain Amino Acid Biosynthesis Pathway

2008 ◽  
Vol 21 (9) ◽  
pp. 1232-1241 ◽  
Author(s):  
Maria de las Nieves Peltzer ◽  
Nicolas Roques ◽  
Véréna Poinsot ◽  
O. Mario Aguilar ◽  
Jacques Batut ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Sinorhizobium Meliloti ◽  
Amino Acid Biosynthesis ◽  
Nodule Formation ◽  
Biosynthesis Pathway ◽  
Acid Biosynthesis ◽  
Branched Chain Amino Acid ◽  
Symbiotic Phenotype ◽  
Branched Chain

Some Sinorhizobium meliloti mutants in genes involved in isoleucine, valine, and leucine biosynthesis were previously described as being unable to induce nodule formation on host plants. Here, we present a reappraisal of the interconnection between the branched-chain amino acid biosynthesis pathway and the nodulation process in S. meliloti. We characterized the symbiotic phenotype of seven mutants that are auxotrophic for isoleucine, valine, or leucine in two closely related S. meliloti strains, 1021 and 2011. We showed that all mutants were similarly impaired for nodulation and infection of the Medicago sativa host plant. In most cases, the nodulation phenotype was fully restored by the addition of the missing amino acids to the plant growth medium. This strongly suggests that auxotrophy is the cause of the nodulation defect of these mutants. However, we confirmed previous findings that ilvC and ilvD2 mutants in the S. meliloti 1021 genetic background could not be restored to nodulation by supplementation with exogenous amino acids even though their Nod factor production appeared to be normal.

Regulation of branched-chain amino acid biosynthesis in Streptomyces fradiae, a producer of tylosin

1989 ◽  
Vol 151 (6) ◽  
pp. 537-540 ◽  
Author(s):  
Aleš Vančura ◽  
Ivana Vančurová ◽  
Jan Kopecký ◽  
Jaroslav Maršálek ◽  
Daniel Cikánek ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Biosynthesis ◽  
Streptomyces Fradiae ◽  
Acid Biosynthesis ◽  
Branched Chain Amino Acid ◽  
Branched Chain

Imazethapyr, an inhibitor of the branched-chain amino acid biosynthesis, induces aerobic fermentation in pea plants

2002 ◽  
Vol 114 (4) ◽  
pp. 524-532 ◽  
Author(s):  
Susana Gaston ◽  
Ana Zabalza ◽  
Esther M. González ◽  
Cesar Arrese-Igor ◽  
Pedro M. Aparicio-Tejo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Biosynthesis ◽  
Acid Biosynthesis ◽  
Aerobic Fermentation ◽  
Branched Chain Amino Acid ◽  
Branched Chain

Herbicides inhibiting branched-chain amino acid biosynthesis

1990 ◽  
Vol 29 (3) ◽  
pp. 241-246 ◽  
Author(s):  
William K. Moberg ◽  
Barrington Cross
Keyword(s):  
Amino Acid ◽  
Amino Acid Biosynthesis ◽  
Acid Biosynthesis ◽  
Branched Chain Amino Acid ◽  
Branched Chain

scholarly journals Branched-chain amino acid biosynthesis inhibitors: Herbicide efficacy is associated with an induced carbon–nitrogen imbalance

2013 ◽  
Vol 170 (9) ◽  
pp. 814-821 ◽  
Author(s):  
Ana Zabalza ◽  
Amaia Zulet ◽  
Miriam Gil-Monreal ◽  
Maria Igal ◽  
Mercedes Royuela
Keyword(s):  
Amino Acid ◽  
Amino Acid Biosynthesis ◽  
Acid Biosynthesis ◽  
Branched Chain Amino Acid ◽  
Biosynthesis Inhibitors ◽  
Branched Chain

scholarly journals Inhibitors of branched-chain amino acid biosynthesis as potential antituberculosis agents

1998 ◽  
Vol 42 (4) ◽  
pp. 475-482 ◽  
Author(s):  
J. A. Grandoni ◽  
P. T. Marta ◽  
J. V. Schloss
Keyword(s):  
Amino Acid ◽  
Amino Acid Biosynthesis ◽  
Acid Biosynthesis ◽  
Branched Chain Amino Acid ◽  
Branched Chain

Cloning of branched chain amino acid biosynthesis genes and assays of α-acetolactate synthase activities in Leuconostoc mesenteroides subsp. cremoris

1999 ◽  
Vol 150 (3) ◽  
pp. 189-198 ◽  
Author(s):  
Jean-François Cavin ◽  
Véronique Dartois ◽  
Cécile Labarre ◽  
Charles Diviès
Keyword(s):  
Amino Acid ◽  
Leuconostoc Mesenteroides ◽  
Acetolactate Synthase ◽  
Amino Acid Biosynthesis ◽  
Acid Biosynthesis ◽  
Branched Chain Amino Acid ◽  
Branched Chain

Acetolactate Synthase and Ketol-Acid Reductoisomerase: Targets for Herbicides Obtained by Screening and de novo Design

1990 ◽  
Vol 45 (5) ◽  
pp. 544-551 ◽  
Author(s):  
John V. Schloss ◽  
Ann Aulabaugh
Keyword(s):  
Amino Acid ◽  
Acetolactate Synthase ◽  
Amino Acid Biosynthesis ◽  
Specific Gene ◽  
Selective Inhibitors ◽  
Acid Biosynthesis ◽  
Threonine Deaminase ◽  
Screening Techniques ◽  
Branched Chain Amino Acid ◽  
Branched Chain

Several major classes of herbicides, discovered by conventional screening techniques, have been found to inhibit the first common enzyme of branched-chain amino acid biosynthesis, acetolactate synthase, as their mode of action. These herbicides seem to bind to an evolutionary vestige of a quinone-binding site, extraneous to the active site, that is present due to the evolutionary history of this enzyme. Besides their herbicidal effect on sensitive plants, these compounds can effect stasis in the growth of bacteria and yeast. Recently is has been reported that an experimental herbicide from Hoechst. Hoe 704. that was discovered by conventional screening techniques, inhibits the second common enzyme of branched-chain amino acid bio- synthesis [Schultz etal., FEBS Lett. 238, 375-378 (1988)]. We have also recently designed novel reaction-intermediate analogs (e.g. N-isopropyl oxalylhydroxamate) that arc exceptionally potent (Ki = 22 pM: half-time for release approximately six days) and selective inhibitors of the second common enzyme, ketol-acid reductoisomerase. Both of these selective inhibitors of the second common enzyme will kill sensitive plants, but will only inhibit the growth (without killing) of bacteria. The effects in bacteria parallel those obtained by mutations in the relevant genes, where loss of either the first or second common enzyme in the pathway gives an organ- ism that is auxotrophic for branched-chain amino acids, but does not result in a conditionally lethal phenotype. Higher plant mutants have only been obtained to date that arc deficient in functional leucine-specific gene products (as yet uncharacterized), threonine deaminase (isoleucine specific), and dihydroxyacid dehydratase (common). The phenotypes of these mutants. at least at the level of cell culture, are similar to those of their bacterial counterparts, in that auxotrophy, but not conditional lethality, is obtained. These results highlight the potential non-equality of the enzymes of branched-chain amino acid biosynthesis as targets in herbicide design.

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