Competitive inhibitors are substances which compete with the substrate by binding to the enzyme's active site, and making the enzyme unavailable to act on the substrate.
In this case, the competitive inhibitor would bind to the enzyme so the the target hydrolysis molecules would not be able to do so.
Non competitive inhibitors act somewhere other than the active site. The react with sites known as 'allosteric sites', or some other sites, which take away the ability of the enzyme to bind to the substrate. That enzyme molecule becomes unable to perform catalysis for the reaction.
OPEN ENDED: In a laboratory a scientist is experimenting with a synthetic enzyme called “hydrolase”. The goal of this enzyme is to bind to intracellular water and speed up hydrolysis RXNs within the cell, so that cells can break apart any polymer at a much faster rate than normal. Describe the mechanisms by which a competitive inhibitor and a non-competitive inhibitor could act on this enzyme.
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