Abstract
Summary Acetohydroxyacid synthase (EC 4.1.3.18) has been extracted from cell suspension cultures of Isatis tinctoria (Cruciferae) and Ruta graveolens (Rutaceae). A combination of salt precipitation, gel filtration and ion exchange chromatography was used for partial purification. The apparent molecular masses of AHAS were Mr 82,000 and 85,000 for Isatis and Ruta, respectively. FAD was an absolute requirement for AHAS activity. The apparent Km values of Isatis-AHAS are the following ones: FAD 6,3 × 10−6 M; TPP 6,3 × 10−6 M; pyruvate 7 × 10−3, and 6 × 10−3 M (for Ruta-AHAS). Branched-chain amino acids and chlorsulfuron are feedback inhibitors for Isatis-AHAS but acetohydroxyacid synthase from Ruta is not sensitive to valine, leucine and isoleucine.
Published Version
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