An enzyme and its substrate are combined in a test tube but no product is formed. Another molecule is added to the tube, and now the product is formed at the normal rate. Give 2 reasons.

I know this has to do with inhibition, but how do I know what kind of inhibition is working on the substrate?

If an allosteric control was added to the tube, it could turn on the enzyme and make it produce a product.

Another thing that could make the product start forming is if a Reversible competitive inhibitor was added, because the inhibition will drop off.

Am I on the right track?