Question

A variety of factors influence enzyme activity. substances that bind to the enzyme and interfere with substrate binding or catalysis are inhibitors. identify the type of inhibition associated with each description and example by classifying them into the appropriate category.

- inhibitor may permanently modify an enzyme
- DIPF permanently modifies the hydroxyl group of a SerSer residue at the active site
- inhibitor binds reversibly to an enzyme's active site
- a transition state analog binds reversibly to isomerase
- inhibitor binds to an enzyme at a site other than the active site
- the Al3+Al3+ ion binds to acetylcholinesterase or to the acetylcholinesterase‑substrate complex

Answer 1

Inhibitors can be classified as irreversible, competitive, or noncompetitive/allosteric based on their interaction with enzymes. Irreversible inhibitors permanently modify the enzyme, competitive inhibitors reversibly bind to the active site, and noncompetitive/allosteric inhibitors bind to another site, changing the enzyme's shape.

Step-by-step explanation:

Enzyme activity can be influenced by various substances, which are classified as inhibitors when they interfere with substrate binding or catalysis. The inhibitors can be grouped based on the nature of their interaction with the enzyme.

Irreversible inhibition: This occurs when an inhibitor permanently modifies an enzyme, such as DIPF permanently modifying the hydroxyl group of a Ser residue at the enzyme's active site.

Competitive inhibition: Exhibited when an inhibitor binds reversibly to an enzyme's active site, competing with the substrate for binding. An example is a transition state analog binding reversibly to isomerase.

Noncompetitive or allosteric inhibition: Occurs when an inhibitor binds to a site other than the active site, such as Al3+ ion binding to acetylcholinesterase or to the acetylcholinesterase-substrate complex, leading to a conformational change that reduces enzyme activity.