The question describes the "induced fit model", in which the binding of a substrate induces an actual change in the shape of the enzyme in order for the substrate to fit properly. This models differs from "the lock and key hypothesis" and "the active site model" (which are actually the same thing, and describes an enzyme and its substrate as fitting perfectly together). Cooperative binding is a concept that refers to binding becoming easier for subsequent molecules in comparison to previous molecules (the sixth molecule binds more readily than the fifth, which binds more readily than the fourth, etc.). Finally, affinity dependent binding is not a real term used in biochemistry (all binding is related to affinity anyway).

A catalyst works to speed up a reaction by lowering the Ea (activation energy), which is related to chemical kinetics. A catalyst has nothing to do with thermodynamics, and can neither change the  of a reaction, nor make a non-spontaneous one occur.

Additionally, by definition a catalyst is not consumed in a reaction, and it is regenerated after the reaction occurs. This allows for the possibility of a catalyst having an enormous impact on the rate of a reaction, as it is can once again exert its effects after being regenerated. 

The most important concept about chronic alcoholism is based off the fact that the increased ratio of  from alcohol metabolism interferes with gluconeogenesis; 2) the conversion of pyruvate to lactate is favored, decreasing gluconeogenesis and increasing blood lactate. Pyruvate dehydrogenase, the enzyme that catalyzes the conversion of pyruvate to lactate. The conversion of pyruvate to acetyl-CoA, catalyzed by alanine aminotransferase, does not require  and is not directly affected by this ratio. An increase in pyruvate to oxaloacetate (catalyzed by pyruvate carboxylase), is a reaction used in gluconeogenesis. If increased, it would favor this process or stimulate the citric acid cycle.

When the body is in a well fed state, insulin stimulates glycolysis (glucose uptake) and the first step to convert glucose to glucose-6-phosphatase.  When you have an increase of insulin, it stimulates protein phosphatase (PP1), which stimulates synthase while inhibiting phosphorylase. This leads to a decreased conversion of glycogen to glucose. Gluconeogeneisis occurs in the starvation state as well as fatty acid degradation.

A first order reaction is one in which the amount of product is dependent on only one reactant. For instance:

The above reaction is first order because the amount of product produced depends solely on the concentration of A. Therefore, a first order reaction is one in which the reaction is directly proportional to the reactant concentration.

Note: bimolecular reaction and second order reaction are synonymous.

A molecule that binds to an allosteric site on an enzyme does not necessarily have a similar structure to the actual substrate. That would only be the case for a molecule that binds to the enzyme's active site. Moreover, the molecule binding to the allosteric site will almost always cause a conformational change in the enzyme's structure, but it can either enhance or inhibit the catalytic activity by doing so.

Zero order reactions are reactions in which the enzyme is saturated with substrate (in first order, the substrate concentration is below Km). The velocity in a zero-order reaction is independent of substrate concentration, therefore the two variables are not related. In a first order reaction, velocity is proportional to substrate concentration.

All of the above statements are true concerning enzymes. They work to lower the activation energy of reactions and do not change the concentrations of substrates or products. They are highly specific and do not get changed by the reaction they are catalyzing.

The fractional saturation of an enzyme is defined as the amount of enzyme that is bound to substrate divided by the total amount of enzyme. To calculate the fractional saturation, we'll need to use the Michaelis-Menton equation:

In addition, we'll need to define the rate and maximum rate in terms of enzyme concentrations:

From the above equations, we can calculate the fractional saturation of the enzyme:

The Michaelis constant, , is not equal to , but is rather the substrate concentration when the reaction rate is .  is an inverse measure of a substrate’s affinity for the enzyme. So as the affinity decreases,  increases. Enzyme specificity is measured by a different constant, , the specificity constant. Although  and specificity are in an inversely proportional relationship,  does not necessarily increase as specificity decreases; rather, , also known as the catalytic constant, could decrease proportionally for a given enzyme. The Michaelis constant, being a measure of affinity, is going to differ for different types of substrates, depending on their shape and other features that influence their ability to bind to an enzyme.