Explain how the position in the active site and function of the oxyanion hole of chymotrypsin supports the theory that enzymes preferentially bind the transition state of the reactions they catalyze

The mechanism of chymotrypsin is used as a model for studying enzyme reaction mechanisms.  Answer the following questions related to chymotrypsin: 1.  List the 3 amino acids in the catalytic triad of chymotrypsin. 2.  List the types of catalytic mechanisms (from the 3 main types of catalytic mechanisms) displayed in the mechanism of chymotrypsin.

The reaction in which glucose 6-phosphate (G6P) is converted to fructose 6-phosphate (F6P) is an example of an isomerization reaction. Notice that both molecules have the molecular formula C6H13O9P. The isomerization is  catalyzed by glucose 6-phosphate isomerase. This is a reversible reaction in cells, with a moderately negative ΔG, but a very high activation energy. If you have a flask that contains a solution containing cellular concentrations of G6P and F6P, but no enzyme, how will the concentration of each molecule change over time?

When regulating phosphofructokinase, why is there such extensive regulation of this reaction and enzymatic reactions, in general?