What does this mean : If a competitive inhibitor (not an allosteric inhibitor) is added to a solution containing such an enzyme, the ratio of enzyme molecules in the active form to those in the inactive form increases.
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What part of this is not clear?
Inhibitors are small molecules which interact with proteins in such a way as to prevent them catalyzing a reaction. These can bind either to the active site - the same site which binds reactants - or to some other part of the protein. When the inhibitor competes with the reactant for the binding site, it's called a competitive inhibitor. When it interacts with some other part of the protein, causing a structural change which prevents the protein from binding its reactant or from carrying through the reaction, it's called an allosteric inhibitor.
Enzymes commonly assume either an active conformation or an inactive conformation. These correspond to actual physical states or shapes the protein assumes. A competitive inhibitor needs physical integrity of the protein to bind - otherwise it won't fit. So it can only bind to the active conformation.
So as the competitive inhibitors bind the active form, a higher proportion of the proteins are stuck or locked in that active conformation because they can't assume the inactive conformation until the inhibitor has dissociated.
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