Regulation of photosynthetic carbon metabolism. The effect of inorganic phosphate on stromal sedoheptulose-1,7-bisphosphatase

The activation and steady-state kinetics of wheat chloroplast sedoheptulose-1,7-bisphosphatase at several concentrations of inorganic phosphate are examined. Inorganic phosphate competitively inhibits substrate binding to both the active and inactive forms of the enzyme and reduces the rate of enzyme activation. Modulation of the apparent Km of sedoheptulose-1,7-bisphosphatase and fructose-1,6-bisphosphatase for their substrates by inorganic phosphate is discussed in terms of the control of intermediate pool sizes in the reductive pentose phosphate pathway and of the flux of fixed carbon towards starch synthesis or export from the chloroplast.