The x-intercept on a Lineweaver-Burk plot tells us the negative reciprocal of .

Because the x-intercept is less negative, this tells us that the inhibited reaction has a larger . Having a different x-intercept but the same y-intercept is characteristic of competitive inhibition. The inhibitor and the substrate are competing for the same binding site. 

Plotting the concentration of the inhibitor versus the concentration of the substrate will not give you any useful information because the reaction rate is essential in determining the type of inhibitor present.

Plotting initial reaction rate versus substrate concentration, or plotting the inverses, describes the graphical representation of Michaelis-Menten kinetics and a Lineweaver-Burk plot, respectively. Both of these are excellent methods to visually determine the type of inhibition displayed. On the graph, the line representing the inhibited enzyme will shift in predictable fashions depending on the type of inhibition. 

Noncompetitive inhibitors bind to enzymes away from the active site (allosteric) and distort it, reducing its affinity for substrate. Since they do not directly compete with substrate for enzyme binding, increasing the substrate concentration in the presence of a noncompetitive inhibitor will have no affect. While enzyme inhibitors include both organic and inorganic molecules, there is not enough information in the question stem to conclude the chemical classification of the inhibitor.

Competitive inhibitors can be overpowered by introducing excess substrate, so they do not affect the maximum rate of the enzyme. They do, however, make it so that more substrate is required in order to get the enzyme working at half of its maximum rate. As a result, competitive inhibitors act by raising the Michaelis constant of enzymes.

A noncompetitive inhibitor acts to decrease how fast the enzyme can act on substrates. It accomplishes this by lowering the maximum rate at which it can create products. Noncompetitive inhibitors do not alter the enzyme's Michaelis constant.

Once in the stomach lumen, pepsinogen finds itself in a very acidic environment. The acidic environment cleaves an amino acid sequence from pepsinogen, turning it into the active enzyme pepsin. This type of activation causes pepsin to only activate in the stomach lumen where it is needed.

Mannose enters glycolysis by first being phosphorylated by hexokinase. The newly formed mannose-6-phosphate is then isomerized into fructose-6-phosphate by the enzyme phosphomannose isomerase. The sugar is now in a form that can follow the normal glycolytic pathway.

If glucose was not phosphorylated, it would be free to diffuse through the plasma membrane and leave the cell. This situation would not be good for the cell because the reaction cannot continue outside of the cytosol. The negative charge created by the phosphorylation prevents the glucose molecule from crossing the plasma membrane due to the similar charge at the plasma membrane. 

Glycolysis can be divided into two parts: the energy investment phase and the energy payoff phase. The energy investment phase comes first when glucose is phosphorylated twice, requiring the use of two molecules of ATP. After the glucose is split, four molecules of ATP will be made in the final steps. This results in a net gain of two ATP in glycolysis, but ATP must be spent prior to being made.

During glycolysis, a total of two molecules of NAD⁺ are reduced in order to form two NADH molecules. These NAD⁺ molecules need to be regenerated in order for more glycolytic reactions to take place; otherwise, the process would come to a halt. Fermentation takes care of this problem in anaerobic environments by oxidizing excess NADH (since it is no longer utilized in the electron transport chain) into NAD⁺, which is then returned to the cytosol where it can be used again in glycolysis.