Results 181 to 190 of about 10,576 (218)

Isolation of acetolactate synthase homologs in common sunflower

Weed Science, 2003
A common sunflower population from Howard, SD (HSD) was previously determined to be cross-resistant to imazethapyr and chlorimuron-ethyl, both acetolactate synthase–inhibiting (ALS) herbicides. Experiments were conducted to determine if target-site polymorphisms could act as a mechanism of ALS-inhibitor herbicide resistance in the HSD common sunflower.
Anthony D. White, Michelle A. Graham, Micheal D. K. Owen   +2 more
openaire   +1 more source

Origin of the herbicide binding site of acetolactate synthase

Nature, 1988
Acetolactate synthase (ALS) is the site of action of several new, structurally diverse classes of herbicides (sulphonylurea1–4, imidazolinone5,6 and triazolo pyrimidine or sulphonanilide7,8). These herbicides are unusual inhibitors in that they bear no obvious similarity to substrates (pyruvate and α-ketobutyrate), cofactors (thiamine pyrophosphate ...
John V. Schloss, Lawrence M. Ciskanik, Drew E.Van Dyk   +2 more
openaire   +1 more source

Catalytic insights of acetolactate synthases from different bacteria

Archives of Biochemistry and Biophysics
Acetolactate synthase (ALS) is an essential enzyme involved in the biosynthesis of platform chemicals acetoin and 2,3-butanediol in several microorganisms. In this study, we investigated the catalytic differences among three bacterial ALSs involved in the ligation of two molecules of pyruvate or 2-ketobutyrate. Based on the findings, we predicted three
Yan-Fei, Liang, Ze-Xin, Niu, Zi-Wen, Wu, Qing-Yang, Zhang, Xin-Yi, Zhao, Lei-Lei, Chao, Heng, Li, Wen-Yun, Gao   +7 more
openaire   +2 more sources

Action mechanisms of acetolactate synthase-inhibiting herbicides

Pesticide Biochemistry and Physiology, 2007
Herbicides that target the acetolactate synthase (ALS) are among the most widely used weed control chemicals since their introduction into the marketplace in the early 1980s, including five classes (sulfonylureas, imidazolinones, triazolopyrimidines, pyrimidinylthio (or oxy)-benzoates and sulfonylamino-carbonyltriazolinones).
Qingyan Zhou, Weiping Liu, Yongsong Zhang, Kevin K. Liu   +3 more
openaire   +1 more source

Roles of lysine 219 and 255 residues in tobacco acetolactate synthase

Biochemical and Biophysical Research Communications, 2002
Acetolactate synthase (ALS) catalyzes the first common step in the biosynthesis of valine, leucine, and isoleucine. The ALS is the target of several classes of herbicides, including the sulfonylureas, the imidazolinones, and the triazolopyrimidines.
Tae-Yeol, Yoon, Sun-Mee, Chung, Soo-Ik, Chang, Moon-Young, Yoon, Tae-Ryong, Hahn, Jung-Do, Choi   +5 more
openaire   +2 more sources

Molecular Mechanism of Enantioselective Inhibition of Acetolactate Synthase by Imazethapyr Enantiomers

Journal of Agricultural and Food Chemistry, 2010
Chiral compounds usually behave enantioselectively in phyto-biochemical processes. Imidazolinones are a class of chiral herbicides that are widely used. They inhibit branched-chain amino acid biosynthesis in plants by targeting acetolactate synthase (ALS).
Qingyan, Zhou, Na, Zhang, Cheng, Zhang, Lidong, Huang, Yaofang, Niu, Yongsong, Zhang, Weiping, Liu   +6 more
openaire   +2 more sources

Structural and Functional Role of Cysteinyl Residues in Tobacco Acetolactate Synthase

Biochemical and Biophysical Research Communications, 2000
Acetolactate synthase (ALS) is the common enzyme in the biosynthesis of valine, leucine, and isoleucine. The role of four cysteinyl residues in tobacco ALS was determined using site-directed mutagenesis and cysteine-specific cleavage. The C411A mutation abolished the enzymatic activity, as well as the binding affinity for the cofactor FAD.
H J, Shin, C K, Chong, S I, Chang, J D, Choi   +3 more
openaire   +2 more sources

[Isolation and purification of acetolactate synthase and acetolactate decarboxylase from a Lactococcus lactis culture].

Prikladnaia biokhimiia i mikrobiologiia, 2000
Enzymes catalyzing the synthesis and subsequent transformation of alpha-acetolactate (AcL)--acetolactate synthase (AcLS) and acetolactate decarboxylase (AcLDC)--were isolated and partially purified from the cells of lactic acid bacteria Lactococcus lactis ssp. lactis biovar. diacetylactis strain 4.
Iu S, Kisrieva, V M, Serebrennikov, N A, Zagustina, A M, Bezborodov   +3 more
openaire   +1 more source

A new synthesis of methyl α-acetolactate based on thiazolium chemistry and modelled on the enzymatic synthesis of α-acetolactate catalysed by acetolactate synthase

J. Chem. Soc., Chem. Commun., 1990
Methyl α-acetolactate [methyl 2-hydroxy-2-methyl-3-oxobutanoate (13)] has been synthesised via a series of adducts with benzothiazole in a manner analogous to the enzymatic reaction catalysed by acetolactate synthase.
David H. G. Crout, Edward R. Lee, David P. J. Pearson   +2 more
openaire   +1 more source

Identification of an acetolactate synthase small subunit gene in two eukaryotes

Gene, 1997
Acetolactate synthase catalyses the first step in branched-chain amino acid biosynthesis. The bacterial enzyme contains two large and two small subunits but there is only limited and circumstantial evidence for a small subunit in the eukaryotic enzyme.
openaire   +4 more sources