Is it possible to do the following:
- Enzyme E binds to its substrate S without catalysis;
- Add a controllable stimulus, such as light, adding or removing chemicals;
- The enzymatic reaction is triggered by the stimulus.
The word controllable means I can add the stimulus at any time I want. Before I add the stimulus, the enzyme keeps binding to the substrate specifically but no reaction takes place.
This is what I mean by separating binding and catalysis in two steps.
In the case of allosteric regulation, some chemicals will inhibit the activity of an enzyme. For example, ATP will inhibit the activity of phosphofructokinase 1 (PFK1). But I'm not sure whether this allosteric inhibition also hinders PFK1's binding to the substrate, which does'nt satisfy my description above.