Phosphofructokinase-1 (PFK-1) is a key regulatory enzyme controlling a major step in glycolysis. Its activity is modulated by allosteric effectors, including activators and inhibitors.
Fructose 2,6-bisphosphate is recognized as a highly potent and physiologically significant allosteric activator of PFK-1. It enhances the enzyme's affinity for fructose-6-phosphate and alleviates inhibition by ATP. This molecule plays a central role in coordinating the rates of glycolysis and gluconeogenesis in response to hormonal signals.
Based on established biochemical regulation, Fructose 2,6-bisphosphate is the most appropriate answer for a potent allosteric activator of PFK-1 among the options.
| Group I | Group II |
| P. 17-$\beta$ estradiol | 1. Arachidonic acid |
| Q. Thromboxane A2 | 2. Tyrosine |
| R. Epinephrine | 3. $\beta$-carotene |
| S. Retinoic acid | 4. Cholesterol |
Which of the following statements are TRUE for respiration?
P. The conversion of one molecule of pyruvate to three molecules of $CO_2$ generates four molecules of NADH
Q. Fructose 6-phospate is the principal substrate for glycolysis
R. The oxidation of glucose 6-phosphate to 6-phosphogluconate is the first step in the oxidative pentose phosphate pathway
S. The mitochondrial 'alternative oxidase' provides an alternative pathway for transfer of electrons from ubiquinone to oxygen utilizing proton pumping complex of the respiratory chain