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Changes in hysteretic kinetics and properties of key regulatory enzymes of wild type & mutant strains of Synechococcus cedrorum during pesticide (endosulfan) stress combat
Abstract
The effects of the hexachlorinated pesticide “endosulfan” on the regulatory kinetics of glucose -6-phosphate dehydrogenase (G6PDH EC 1.1.1.49) from wild type (WT) and pesticide resistant mutant type (EndR) strains of the cyanobacterium Synechococcus cedrorum were analysed. G6PDH from both strains was a “hysteretic” enzyme which could exist either in the aggregated “hyperactive” form which had an initial burst of activity or in the dissociated “hypoactive” form. The Km values for substrate G6P were 0.83 and 0.96 µM in WT and EndR strains, respectively. Hyperactivity following growth in endosulfan increased in the EndR strain whereas it decreased in the WT strain. These changes were accompanied by synthesis of a new class of membrane localized proteins with molecular weights of about 70-80 kDa The Km of nitrate reductase of wild type and mutant strains were observed to be 15.3 and 29.4 µM, respectively. This was concomitant with phycobilisome disintegration in the wild type only, diagnostic of nitrogen deficiency. The results taken together point to a coordination of carbon and nitrogen metabolism during endosulfan stress combat emphasizing the role of global regulatory networks of the metabolome.
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