Abstract
1. 1. 6-Phosphogluconate, 3-phosphoglycerate and 2-phosphoglycerate were allosteric modifiers fo pea-sed phosphofructokinase (ATP: D-fructose 6-phosphate 1-phosphotransferase, EC 2.7.1.11) and each inhibited enzyme activity. The inhibitions were relieved by increasing the concentration of fructose 6-phosphate or by lowering the ATP concentration. In the presence of P i, at low ATP concentrations, 6-phosphogluconate, 3-phosphoglycerate and 2-phosphoglycerate stimulated phosphofructokinase activity. 2. 2. Experiments with other intermediates of carbohydrate metabolism showed that 2,3-diphosphoglycerate inhibited pea-seed phosphofructokinase, but glucose 6-phosphate, pyruvate, succinate and malate had no effect. 3. 3. A common mechanism is suggested for the interaction of 6-phosphogluconate, 3-phosphoglycerate, 2-phosphoglycerate and phosphoenolpyruvate with the enzyme molecule. 4. 4. The possible significance of these modifiers of pea-seed phosphofructokinase in the regulatory control of plant carbohydrate metabolism is discussed.
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