Results 161 to 170 of about 5,600 (215)

Development of herbicide-resistant peanut via prime editing and optimization of editing efficiency. [PDF]

Plant Physiol
Xue L, Qu P, Zhao H, Liu H, Li X, Wang X, Huang B, Han S, Dai X, Dong W, Shi L, Zhang X.   +11 more
europepmc   +1 more source

Systematically Engineering for Efficient Production of 3-Methyl-1-Butanol in Escherichia coli. [PDF]

Adv Sci (Weinh)
Geng N, Liu H, Han H, Meng M, Wang S, Tan T, Su H.   +6 more
europepmc   +1 more source

Plug-and-play - enzymatic amino acid production from methanol and carbon dioxide. [PDF]

Nat Commun
Willers VP, Lehmann V, Müller S, Vogelgsang F, Roth A, Blombach B, Pick A, Sieber V.   +7 more
europepmc   +1 more source

Resistance to acetolactate synthase (ALS) inhibiting herbicides in UK populations of the grass-weed Alopecurus myosuroides (black-grass)

, 2007
Moss, S. R., Marshall, R.
core  

The oxygenase reaction of acetolactate synthase detected by chemiluminescence [PDF]

FEBS Letters, 1994
In addition to the synthesis of ketolacids the enzyme acetolactate synthase shows an oxygen‐consuming side reaction. Partially purified acctolactate synthase from corn (Zea mays L.) and barley (Hordeum vulgare L.) exhibits chemiluminescence in the presence of oxygen, Mn2+ and low concentrations of pyruvate. Light emission is inhibited by azide, but not
Peter Boger
exaly   +4 more sources

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The oxygenase reaction of acetolactate synthase

Biochemistry, 1993
In addition to the physiological reactions catalyzed by acetolactate synthase, it supports an oxygen-consuming side reaction. Although the synthase and oxygenase activities are activated to somewhat different extents by various metals (Mn2+, Mg2+, Ca2+, Co2+, Zn2+, Ni2+, Cd2+, Cu2+, Ba2+, Al3+), the modest degree of these differences (at most 6-fold ...
M T, Tse, J V, Schloss
openaire   +2 more sources

Roles of Histidine Residues in Tobacco Acetolactate Synthase

Biochemical and Biophysical Research Communications, 2001
Acetolactate synthase (ALS) catalyzes the first common step in the biosynthesis of valine, leucine, and isoleucine in plants and microorganisms. ALS is the target of several structurally diverse classes of herbicides, including sulfonylureas, imidazolinones, and triazolopyrimidines.
K J, Oh, E J, Park, M Y, Yoon, T R, Han, J D, Choi   +4 more
openaire   +2 more sources

Synthesis of Indolosulfonylureas, Potent Acetolactate Synthase Inhibitors.

ChemInform, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Ye Zhang, Tianrui Ren
openaire   +1 more source

Acetolactate Synthase Inhibitors

2002
Acetolactate synthase (ALS; EC 4.6.3.8, also referred to acetohydroxy acid synthase; AHAS) is the first common enzyme in the biosynthetic pathway to the branched-chain amino acids; valine, leucine and isoleucine (Fig. 1). The pathway exists in plants and microorganisms such as bacteria, fungi and algae.
Tsutomu Shimizu, Ishizue Nakayama, Kozo Nagayama, Takeshige Miyazawa, Yukio Nezu   +4 more
openaire   +1 more source

Role of Tryptophanyl Residues in Tobacco Acetolactate Synthase

Biochemical and Biophysical Research Communications, 1999
Acetolactate synthase (ALS) catalyzes the first common step in the biosynthesis of valine, leucine, and isoleucine. ALS is the target of three classes of herbicides, the sulfonylureas, the imidazolinones, and the triazolopyrimidines. Five mutants (W266F, W439F, W490F, W503F, and W573F) of the ALS gene from Nicotiana tabacum were constructed and ...
C K, Chong, H J, Shin, S I, Chang, J D, Choi   +3 more
openaire   +2 more sources