1. Iodoacetamide combines with the thiol group of cysteine, thus, the protein cannot produce a disulfide bond. So, iodoacetate is an inhibitor of cysteine peptidase.
2. In the presence of competitive inhibition, the Km increases. In the presence of a competitive inhibitor -1/Km increases, thus, 1/Km decreases, and hence Km increases. The competitive inhibitors work by combining reversibly with the active site of an enzyme. Thus, more concentration of substrate is required to attain half of the maximum velocity.
3. In the given case, half of the molecules of the enzyme are completely active and half of the molecules of the enzyme are completely inactive.
Irreversible inhibition is one of the reasons for the reduction in the rate of an enzyme-catalyzed reaction in the given case. The loss of activity of the enzyme molecules due to irreversible inhibition is time dependent and it is the reason behind the reduction in reaction rate.
Reduction in the rate of reaction is proportional to the loss of activity. Therefore, a 50 percent reduction in reaction rate will result in 50 percent of the enzyme molecules to be inactive and the other 50 percent of the enzyme molecules to be completely active.
4. The statement, that is, in the majority of the cases, the inhibitor can be removed by dialysis is not true about irreversible enzyme inhibitors.
The irreversible inhibitors combine with the enzymes permanently and make covalent bonds with the enzyme. Therefore, it cannot get removed by the process of dialysis in the majority of cases.
5. The correct statement is that the initial velocity increases in the presence of an enzyme.
6. The correct statement is that the Vmax is attained when the concentration of the substrate is double the Km.
The Km is illustrated as the concentration of substrate at which the reaction velocity reaches half of the maximum velocity. Therefore,
Km = 1/2 Vmax
2 Km = Vmax
Vmax = 2 Km