Question

which of the following best describes an example of how an enzyme inhibitor can work in a reaction catalyzed

Answer 1

In general terms, an inhibitor is a small molecule which binds to the enzyme and prevents it from catalyzing the reaction. Some do this by binding to and blocking the active site, others do this by binding some other part of the enzyme and changing either its structure or its dynamics (how it moves) so that it can't catalyze the reaction...

Answer 2

yes like what @blues said, inhibitors basically inhibits a reaction, there are two types of inhibitors though, competitive and non-competitive. Competitive inhibitors normally compete with substrate for the enzyme's active site and its normally reversible.

Non-competitive inhibitors on the other hand, attaches to other parts of the enzyme apart from the active site, (allosteric site) and it's irreversible. So what happens after that is mentioned by blues already :)