Results 161 to 170 of about 10,495 (222)

Using BONCAT to dissect the proteome of <i>S. aureus</i> persisters. [PDF]

mSphere
George Matlalcuatzi EDC, Bakkum T, Thomas PS, Hacker S, Florea BI, Vriesendorp B, Rozen DE, van Kasteren SI.   +7 more
europepmc   +1 more source

Molecular mechanisms of disinfectant resistance in <i>Klebsiella pneumoniae</i>. [PDF]

JAC Antimicrob Resist
Noel DJ, Bailey A, Nicholas BI, Skipp P, Keevil CW, Wilks SA.   +5 more
europepmc   +1 more source

Complete genome sequence of <i>Serratia nematodiphila</i> G5.M166, an antifungal soil isolate from Hong Kong. [PDF]

Microbiol Resour Announc
Ng CHN, Leung KM, Lai GKK, Griffin SDJ.
europepmc   +1 more source

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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

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

An in vivo Acetolactate Synthase Assay

Weed Technology, 1995
A method was developed and tested for in vivo assay of acetolactate synthase (ALS). The method used foliar application of 1,1-cyclopropanedicarboxylic acid (CPCA) to inhibit ketol-acid reductoisomerase, the enzyme immediately following ALS in biosynthesis of branched-chain amino acids, thereby causing accumulation of acetolactate.
David M. Simpson, Edward W. Stoller, Loyd M. Wax   +2 more
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

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

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