Flavin adenine dinucleotide causes oligomerization of acetohydroxyacid synthase from black Mexican sweet corn cells

@inproceedings{Singh1989FlavinAD,
  title={Flavin adenine dinucleotide causes oligomerization of acetohydroxyacid synthase from black Mexican sweet corn cells},
  author={Bijay K. Singh and Gail Schmitt},
  year={1989}
}
Abstract Acetohydroxyacid synthase activity is stabilized and stimulated by flavin adenine dinucleotide. Flavin adenine dinucleotide was found to cause aggregation of acetohydroxyacid synthase from the dimeric to a tetrameric form. The different aggregation states of the enzyme have differential sensitivities to inhibition by branched chain amino acids as well as by imazapyr, an imidazolinone herbicide. These observations indicate that flavin adenine dinucleotide is of structural as well as of… CONTINUE READING