Regulatory role of polyamine in the acid phosphatase from potato tubers

摘要: Abstract Effects of polyamine and metal ions on the new type acid phosphatase purified from potato ( Solanum tuberosum L. Irish Cobbler) tubers were analyzed. The enzyme belongs to nonspecific family (EC 3.1.3.2), which hydrolyzes various phosphorylated substrates. hydrolyzed inorganic pyrophosphate as a preferred substrate, exhibited hyperbolic kinetics with respect in absence cations. Polyamine activated effectively by lowering K m value without appreciable changes maximal velocity. most effective polyamines activators spermine spermidine. Mg 2+ ion increased affecting velocity enzyme, but Ca decreased both V max values. Increasing concentrations also irrespective included, gave constant values presence ion. Action can be explained complex formation substrate pyrophosphate. utilize pyrophosphate–spermine or pyrophosphate–Ca However, use pyrophosphate–Mg weak affinity for active site. activates cations, activation may contribute stimulation starch biosynthesis control glycolysis/gluconeogenesis regulating PPi levels growing tubers.