Pesticide inactivation of peanut glutamate dehydrogenase: Biochemical basis of the enzyme's isomerization
Journal of Agricultural and Food Chemistry
Glutamate dehydrogenase (GDH) isomerizes in response to pesticides and environmental chemicals, but the biochemical basis of the isomerization is not known. Clearer understanding of the isomerization would permit expansion of its utility in the diagnosis of the responses of plant tissues to challenged environments. Peanut plants were treated with different rates of Basagran (3-(1-methylethyl)-1H-2,1,3-benzothiadiazin-4(3H)-one 2,2-dioxide), Bravo 720 (tetrachloroiso-phthalonitrile), and Sevin XLR Plus (1-naphthyl N- methylcarbamate). Free solution isoelectric focusing, followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) fractionated the peanut seed GDH to its constituent subunits and degradation polypeptides. After western transfer to nitrocellulose membrane, the GDH subunits and degradation polypeptides were immunodetected with anti-GDH. The pesticide treatments did not induce increased proteolytic activity, but induced about 50% degradation of the GDH, whereas the GDH of the control peanut suffered only about 25% degradation, thus showing that the degradation rate was about double the rate of de novo synthesis in the pesticide treatments. The heavy displacement of the GDH subunit equilibrium toward degradation explains the biochemical basis of the isomerization reaction.
Osuji, G., Braithwaite, C., Pointer, R., & Reyes, J. (1999). Pesticide inactivation of peanut glutamate dehydrogenase: Biochemical basis of the enzyme's isomerization. Journal of Agricultural and Food Chemistry, 47 (8), 3345-3351. https://doi.org/10.1021/jf980531v