Results 171 to 180 of about 5,600 (215)

Intraspecific variability of the acetolactate synthase gene

Weed Science, 2004
Common ragweed and common cocklebur plants were collected at two sites each in Illinois, Minnesota, and Ohio to analyze intraspecific variability of the gene encoding acetolactate synthase (ALS). A 385-nucleotide fragment within the coding sequence ofALSwas compared among 24 plants of each of these two species from the six locations.
Patrick J. Tranel, Weilu Jiang, William L. Patzoldt, Terry R. Wright   +3 more
openaire   +1 more source

A basal unit of valine-sensitive acetolactate synthase of Neurosporacrassa

Biochemical and Biophysical Research Communications, 1984
Valine-sensitivity as well as activity of acetolactate synthase of Neurospora crassa was stabilized with 1.2 M potassium phosphate buffer during extraction from mitochondria and early stages of purification, and with 20% glycerol plus 5 mM sodium pyruvate during Sephadex G200 gel chromatography. The enzyme was expressed as four molecular species having
Homare Kuwana
exaly   +3 more sources

Roles of conserved methionine residues in tobacco acetolactate synthase

Biochemical and Biophysical Research Communications, 2003
Acetolactate synthase (ALS) catalyzes the first common step in the biosynthesis of valine, leucine, and isoleucine. ALS is the target of several classes of herbicides, including the sulfonylureas, the imidazolinones, and the triazolopyrimidines. The conserved methionine residues of ALS from plants were identified by multiple sequence alignment using ...
Dung, Tien Le, Moon-Young, Yoon, Young Tae, Kim, Jung-Do, Choi   +3 more
openaire   +2 more sources

The acetolactate synthase isoenzymes of Escherichia coli K-12

Molecular and General Genetics MGG, 1977
Strains of Escherichia coli K-12 possessing only one of the three genes coding for acetolactate synthetase activity present either in the wild type or in its ilv0603 derivative were prepared and analyzed. Extracts prepared from these strains show different values of acetolactate synthase specific activity and different sensitivity to valine inhibition.
J, Guardiola, M, De Felice, A, Lamberti, M, Iaccarino   +3 more
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Resistance To Acetolactate Synthase Inhibiting Herbicides

2018
One of the most significant occurrences in herbicide resistance has been the advent of weeds resistant to herbicides that inhibit acetolactate synthase. The topic of herbicide-resistant crops in agriculture has been reviewed by B. J. Mazur and S. C. Falco.
L. L. Saari, J. C. Cotterman, D. C. Thill   +2 more
openaire   +1 more source

Isolation and purification of acetolactate synthase and acetolactate decarboxylase from the culture ofLactococcus lactis

Applied Biochemistry and Microbiology, 2000
Enzymes catalyzing the synthesis and subsequent transformation of α-acetolactate (AcL)—acetolactate synthase (AcLS) and acetolactate decarboxylase (AcLDC)—were isolated and partially purified from the cells of lactic acid bacteriaLactococcus lactis ssp.lactis biovar.diacetylactis, strain 4.
Yu. S. Kisrieva, V. M. Serebrennikov, N. A. Zagustina, A. M. Bezborodov   +3 more
openaire   +1 more source

Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1998
Two groups of enzymes are classified as acetolactate synthase (EC 4. 1.3.18). This review deals chiefly with the FAD-dependent, biosynthetic enzymes which readily catalyze the formation of acetohydroxybutyrate from pyruvate and 2-oxobutyrate, as well as of acetolactate from two molecules of pyruvate (the ALS/AHAS group).
D, Chipman, Z, Barak, J V, Schloss
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Effect of Gliotoxin and Related Compounds on Acetolactate Synthase

Journal of Agricultural and Food Chemistry, 1997
Gliotoxin (1), a fungal metabolite, inhibited acetolactate synthase (ALS), one of the targets of commercial herbicides. The inhibitory effect of gliotoxin was more potent against yeast ALS than against tobacco cells. The ALS inhibitory activity of gliotoxin was considered to be associated with the 1,4-dione moiety.
Hiroyuki Haraguchi, Kaori Yamano, Naoko Kusunoki, Ayumi Fukuda   +3 more
openaire   +1 more source

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