can someone help me out by comparing enzyme denaturation and enzyme inhibition?

Answer 1

when an enzyme is denatured, it has been heated to a degree where cooling it won't turn it back, which will usually make the enzyme useless
for example: you add heat to an egg and fry it, when u put it back in the freezer does it turn back into the liquid yoke that was in the egg before?

inhibition involves an inhibitor either binding directly into the active site or binding to a different site causing the enzyme to change shape and no be able to complete the action it was meant to do

hope this helps you out

Answer 2

Denaturation, in effect, destroys the enzyme. Sometimes it can be reversible, especially if the temperature is very near the denaturation point, but by and large, the enzyme is rendered completely non-fucntional.

Inhibition is caused by a molecule that binds to the enzyme and halts its activity. Once the inhibitor is cleared away, though, activity resumes. Alternatively, an enzyme can be inhibited competitively. The competitor would have a higher affinity or concentration than the normal substrate. When present, the enzyme would catalyze a reaction with the competitor, rather than its normal substrate.

In the end, both are valid methods of stopping a reaction, but the difference is in speed and reversibility. Inhibition is very quick and easy, and is reversible, but requires the presence of an inhibitor. For the most part, denaturation is permanent.