How to Phosphofructokinase-1 (PFK-1) and Fructose 1,6-Bisphosphatase are reciprocally regulated ?a) ATP inhibits PFK-1 by binding to an allosteric site and lowering the affinity of the enzyme for its substrate fructose 6-phosphateb) citrate is also an allosteric regulator of PFK-1, high citrate concentration increases the inhibitory effect of ATPc) FBPase-1, is strongly inhibited (allosterically) by AMP; when the cell’s supply of ATP is low (corresponding to high AMP), the ATP-requiring synthesis of glucose slowsd) AMP inhibits PFK-1 by binding to an allosteric site and lowering the affinity of the enzyme for its substrate fructose 6-phosphateWhich of the following statements of regulation of enzyme is correct? -triyambak.org