Question

Explain enzyme inhibition
(In basic terms because this is a biology 101 class)

Answer 1

Enzyme inhibitors can reduce or stop the rate of enzyme-catalyzed reactions by binding to enzymes. They exist as irreversible inhibitors, which permanently inactive the enzyme, and reversible inhibitors, which include competitive and noncompetitive types that bind temporarily.

Step-by-step explanation:

Enzyme inhibitors are substances that bind to enzymes and reduce their catalytic activity, effectively decreasing the rate of enzyme-catalyzed reactions. These inhibitors can be classified into two main types: irreversible and reversible.

Irreversible inhibitors bind to an enzyme in such a way that it cannot be removed; the binding is permanent, and the enzyme is permanently inactivated. This is akin to enzyme 'poisoning'.

Reversible inhibitors can bind to enzymes temporarily. There are two subclasses: competitive inhibitors and noncompetitive inhibitors. Competitive inhibitors compete with the substrate for the active site of the enzyme. They can be outcompeted by a high concentration of substrate. Noncompetitive inhibitors, however, bind to a different part of the enzyme and change its shape, which affects enzyme activity even if the substrate concentration is high.

One well-known inhibitor is aspirin, which selectively inhibits an enzyme involved in synthesizing molecules that trigger inflammation.

Answer 2

A chemical that prevents an enzyme from working. Enzymes participate in a variety of cell processes, such as cell signaling, growth, and division, as well as accelerating chemical reactions in the body. Enzyme inhibitors may be used in the treatment of cancer to prevent the growth of particular enzymes required by cancer cells.