Enzymes

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between and substrate appears to alter the shape of the enzyme. This induces a close fit between the active site and the substrate. It is also believed that this may put some strain on the substrate molecule facilitating the reaction.
Another characteristics of are competitive inhibition and non-competitive inhibition. Competitive inhibition is the binding of a competitive molecule to the active site of the enzyme. This prevents the proper substrate from reacting with the enzyme. In non-competitive inhibition the binding of a non-competitive inhibitor to another site on the enzyme induces an allosteric change, or conformational change, that prevents the active site from binding to the proper substrate. An allosteric change could be either a negative modulator or a positive effector. There’s also cooperativity. This is the binding at an active site that makes the others more reactive. An example to this is hemoglobin. Co- are also factors of . These are ...

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