Regulation of ADPglucose pyrophosphorylase in cucumber plants infected with the cucumber mosaic virus

ADPglucose pyrophosphorylase level and mechanisms regulating its activity were studied in cucumber plants infected with the cucumber mosaic virus at the stage of chronic infection. Studies carried out with partially purified preparations of the enzyme have shown that there was no substantial difference in the regulatory influence of the ratio 3-PGA/P₁, or in the number of binding sites of the effectors on the enzyme, but that the virus infection reduced the level of the enzyme in the tissues to 74% of the control and the 3-PGA/P₁ ratio to one half which resulted in a further decrease in ADPglucose pyrophosphorylase activity. In crude homogenate prepared from diseased plants, activity of the enzyme was reduced to 42% of the healthy control. The level of UDPglucose pyrophosphorylase was three times higher in cucumber leaf tissues than the level of ADPglucose pyrophosphorylase which was inhibited by both 3-PGA and P₁. Inhibitory effects of both these effectors were cumulated. The enzyme isolated from healthy plants was inhibited by inorganic phosphate more strongly than the enzyme isolated from diseased plants. UDPglucose pyrophosphorylase activity was increased in crude homogenate of diseased plants to 127% of the healthy control when the level of the enzyme was the same in the tissues of both healthy and diseased plants which was presumably connected with the enhanced rate of sucrose catabolism.