The oxidation of glucose to two molecules of pyruvate produces a net two molecules of ATP during glycolysis. ATP allosterically inhibits the enzyme, PFK-1, that catalyzes the third step of glycolysis. This is an example of which fo the following mechanisms?

Based on the following lineweaver-burk plot shown below, what type of inhibition is occurring?

Consider the given Lineweaver-Burk plot, showing the inhibition of an enzyme.

Based on this graph, which of the following is a true statement?

Transition state analogs are generally used as what kind of inhibitors for enzymes?

In which type of inhibition does the inhibitor bind to both the free enzyme and the enzyme-substrate complex with equal affinity?

A researcher is analyzing a molecule. Upon addition of this molecule to an enzymatic reaction, he notices that the reaction slows down. He is, however, able to bring the reaction back to normal speed after addition of more substrates. What can you conclude about this molecule?

I. It is a competitive inhibitor

II. It decreases

III. It decreases

Complete the statement about enzymatic inhibition:

In __________ inhibition, the inhibitor can only bind to a complex of the enzyme and its substrate (ES complex). As a result of this type of inhibition, __________.

Suppose that for a given enzymatic reaction, the addition of a certain chemical was found to result in a reduction in both the maximum reaction rate (), as well as the concentration of substrate necessary to achieve half the maximum rate (). Which of the following phrases best describes this added chemical?

What type of inhibition increases without changing ?

Match the type of inhibition with the appropriate change in either or .