Regulatory role of polyamine in the acid phosphatase from potato tubers.

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

Dipicolinic acid prevents the copper-dependent oxidation of low density lipoprotein.

Effect of dipicolinic acid (pyridine 2,6-dicarboxylic acid) and pyridine compounds on the copper-dependent oxidation of human low density lipoprotein was analyzed in relation to the inhibition of copper reduction. Dipicolinic acid inhibited copper-dependent LDL oxidation completely, but the LDL oxidation was slightly inhibited by pyridine compounds with one carboxyl group at 2 or 6-position. Reduction of copper by LDL itself and ascorbate was inhibited completely by dipicolinic acid, but only partially by picolinic acid, quinolinic acid and isocinchomeronic acid with 2- or 6-carboxylic group. Pyridine compounds without 2- or 6-carboxyl group did not show any inhibitory effect on the LDL oxidation and the copper reduction. Protective effect of dipicolinic acid on the LDL oxidation was closely correlated with the copper-reducing activity. Dipicolinic acid shows an antioxidant action by the formation of a chelation complex with copper. This may have implications in understanding mechanisms of preventing LDL oxidation during the early phase of atherosclerosis.