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Because more substrate-occupied active sites are present, competitive inhibition will be reduced,predicts the effect of increasing the concentration of substrate (ethyl alcohol), while keeping the concentration of the inhibitor (methyl alcohol) constant.
Enzymes are biochemical catalysts that support biochemical reactions in living cells.Their core 3D protein structures, known as their active sites, are used to bind with substrates during reactions.Enzyme processes are typically impacted by inhibitors (such as methyl alcohol), which compete with the true substrate (ethyl alcohol) for the active site.An illustration of competitive inhibition might be this. Since there is more ethyl alcohol accessible, there are more active sites occupied, which reduces the possibility that the inhibitor methyl alcohol will bind to the active site and prevent the creation of harmful formaldehyde and more non-toxic compounds from forming at the active sites.
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