So if you don't remember what this does, go back to the previous lecture and check that out and notice this one is inactivated in state A. Now, when we go to state B, when protein kinase A phosphorylates the serial residue to form this phosphorylated state, we see that that deactivates this molecule, the PFK two, while activating that fructose bisphosphatase two. And what the fructose bisphosphatase two does is it basically reverses what this phosphorctocinase two actually does. And that's why we say they have a reciprocal function, they're opposite in what they actually do. So now what happens is the FDPH too, because it's active, it causes the defasphorylation, it removes that phosphoryl group from that fructose, fructose two six bisphosphate to form that fructose six phosphate. So now that we know what this key element is, the fact that we have this bifunctional allosteric enzyme found in the liver, in kidney cells that basically is used to regulate this process of glycolysis and gluconeogenesis, let's actually see how this all takes place.