Statement I is false because increasing the substrate concentration will only help overcome competitive inhibition. Noncompetitive inhibition can only be overcome if the inhibitor is removed from the enzyme.

Statement II is also false because competitive inhibitors do not change the active site. They bind to the active site and prevent substrates from binding. Noncompetitive inhibitors bind elsewhere on the enzyme and alter the shape of the active site, thereby preventing substrate binding.

Statement III is true because noncompetitive inhibition does not affect the enzyme affinity for substrates. The enzyme still has the same affinity, but the substrates can’t bind because of the altered active site.

Negative feedback interrupts a metabolic pathways by producing a substrate that inhibits enzymes in the beginning steps of the metabolic cycle. If a chemical is "mimicking" substrate C  or causing Substrate C to be produced before other steps in a cycle, the enzyme is inhibited by the excess of substrate C thus the pathway can not continue. Most such molecules are proteins that interact with enzymes. 

A substrate that acts as a "positive motivator" of, or to enhance a metabolic pathway, is also known as a positive feedback regulator or a substance that has a positive feedback mechanism.

Competitive inhibition occurs when an substrate or inhibitor compete with the normal substrate for binding the active sight of an enzyme. The proper functioning of the enzyme depends on the concentration ratio of inhibitor to enzyme or substrate to enzyme. The competitive inhibition of the enzyme in this case by the antibiotic has potentially bactericidal or bacteriostatic effect on the bacteria until that antibiotic concentration decreases. Negative feedback involves the product of a set of metabolic reactions inhibiting the formation of a precursor of that metabolic pathway, thereby decreasing its own production.

Noncompetitive inhibition is a type of enzymatic alteration that results in changes to enzymatic function without alterations to the active site. If the active site was to be blocked, this compound would function via competitive inhibition. The other terms do not describe any type of enzymatic inhibition process in the human body. Be able to distinguish the difference between competitive and noncompetitive inhibition.

The temperature and pH of the environment, as well as the concentration of the substrate and enzyme, all affect the rate at which an enzyme catalyzes a reaction. As a result, enzymes have optimal conditions in which they can work at peak efficiency.

Enzymes are catalysts that help a reaction proceed faster. Increasing the concentration of carbonic anhydrase will not cause the reaction to go slower. Recall that catalysts (in this case carbonic anhydrase) do not alter the equilibrium of a reaction. They simply speed up the process so that equilibrium can be achieved more quickly. Increasing or decreasing the equilibrium constant means that there is a change in the equilibrium state of the reaction.

The equilibrium constant can only be affected by temperature changes or pressure changes, if there is a gas involved in the reaction. Catalysts affect the rate constant, which is dependent on activation energy. By decreasing activation energy, catalysts can increase the rate constant and allow a reaction to proceed faster.

There is an optimum temperature at which an enzyme is most effective. Decreasing or increasing the temperature from the optimum will lead to denaturation of proteins, which will affect their functionality. Most protein structure is dependent on non-covalent intermolecular forces, such as hydrogen bonding and hydrophobic interactions. Heat can disrupt these forces, causing the protein to lose its structure, which leads to a loss of functionality.

You can eliminate the answer choices about activation energy because changing temperature will have no effect on the activation energy. Adding heat could shift the equilibrium to the right or left, depending on whether the reaction is exothermic or endothermic.

Temperature, pH, and substrate concentration all affect the function of an enzyme; therefore, the correct answer is all of these.

The correct answer to this question is they function under a narrow pH range.

Enzymes do indeed function under a narrow pH range. A narrow pH range is needed because enzymes speed up reactions by lowering the activation energy and in order to do this very specific conditions must be met. Coenzymes are not always needed and they are certainly not consumed in a reaction. Enzymes also are proteins so they are polymers of amino acids, not carbohydrates. Also enzymes have no part in the creation of ATP.