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Expression of acetohydroxyacid synthase from Bacillus anthracis and its potent inhibitors

Title
Expression of acetohydroxyacid synthase from Bacillus anthracis and its potent inhibitors
Authors
Choi K.-J.Chien N.P.Jung H.Han S.-H.Choi J.-D.Kim J.Yoon M.-Y.
Ewha Authors
김진흥
SCOPUS Author ID
김진흥scopus
Issue Date
2007
Journal Title
Bulletin of the Korean Chemical Society
ISSN
0253-2964JCR Link
Citation
vol. 28, no. 7, pp. 1109 - 1113
Indexed
SCI; SCIE; SCOPUS; KCI WOS scopus
Abstract
Acetohydroxyacid synthase (AHAS, EC 2. 2. 1. 6) is the enzyme that catalyses the first step in the common pathway of the biosynthesis of the branched chain amino acids, valine, leucine and isoleucine. For the first time, the AHAS gene from Bacillus anthracis was cloned into the expression vector pET28a(+), and was expressed in the E. coli strain BL21(DE3). The purified enzyme was checked on 12% SDS-PAGE to be a single band with molecular weight of 65 kDa. The optimum pH and temperature for B. anthracis AHAS was at pH 7.5 and 37 °C, respectively. Kinetic parameters of B. anthracis were as follows: Km for pyruvate, K0.5 for ThDP and Mg2+ was 4.8, 0.28 and 1.16 mM respectively. AHAS from B. anthracis showed strong resistance to three classes of herbicides, Londax (a sulfonylurea), Cadre (an imidazolinone), and TP (a triazolopyrimidine). These results indicated that these herbicides could be used in the search for new anti-bacterial drugs.
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자연과학대학 > 화학·나노과학전공 > Journal papers
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