期刊论文详细信息
FEBS Letters
Flavin adenine dinucleotide causes oligomerization of acetohydroxyacid synthase from black Mexican sweet corn cells
Singh, Bijay K.1  Schmitt, Gail K.1 
[1] American Cyanamid Company, P.O. Box 400, Princeton, NJ 08540, USA
关键词: Acetohydroxyacid synthase;    Flavin adenine dinucleotide;    Imidazolinone;    Sulfonylurea;    AHAS;    acetohydroxyacid synthase;    FAD;    flavin adenine dinucleotide;    TPP;    thiamine pyrophosphate;    PBS;    phosphate buffered saline;   
DOI  :  10.1016/0014-5793(89)81628-X
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

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 functional importance for the plant acetohydroxyacid synthase enzyme.

【 授权许可】

Unknown   

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