Abstract
Pyruvate dehydrogenase phosphatase requires Mg 2+ or Mn 2+, and its activity in the presence of Mg 2+ is markedly stimulated by Ca 2+. At saturating Mg 2+ and Ca 2+ concentrations, the polyamines spermine, spermidine and putrescine stimulated the activity of pyruvate dehydrogenase phosphatase 1.5- to 3-fold. Spermine was the most active of the polyamines. At a physiological concentration of Mg 2+ (1 mM) and saturating Ca 2+ concentration, the stimulation by 0.5 mM spermine was 4- to 5-fold, and at 0.3 mM Mg 2+, the stimulation was 20- to 30-fold. In the absence of Mg 2+ or Ca 2+, spermine had no effect. These results suggest that a polybasic factor may be involved in the regulation of pyruvate dehydrogenase phosphatase activity.
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