Expression of acetohydroxyacid synthase from Bacillus anthracis and its potent inhibitors

Kyoung Jae Choi, Ngoc Pham Chien, Hoeil Jung, Sung Hwan Han, Jung Do Choi, Jinheung Kim, Moon Young Yoon

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12 Scopus citations


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.

Original languageEnglish
Pages (from-to)1109-1113
Number of pages5
JournalBulletin of the Korean Chemical Society
Issue number7
StatePublished - 20 Jul 2007


  • Acetohydroxyacid synthase
  • Herbicides
  • Kinetic parameters
  • Resistance


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