Answer:
it is considered non-competitive mainly because the inhibitor does no resemble the substrate that is ae to fit into the active site so it binds to the allosteric site, if it bonds to the active site then it has competition from actual substrates to fit in the active site
Step-by-step explanation:
and from the metabolic pathway, we know that most likely the size of molecule A is greater than that of E since A has to be broken down through several reactions before E is produced, from this we would know that E would not resemble the structure or size of A and hence would not be able to fit in the active site of the enzyme that catalyzed A to B. From this we can deduct that the only possible thing would have been that it inhibited the allosteric site and is therefore non- competitive