By binding to enzymes’ active sites or allosteric sites, inhibitors reduce the compatibility of substrate and enzyme and this leads to the inhibition of Enzyme-Substrate complexes’ formation, preventing the production of the product<\/div><\/p>\n\n\n\n Between the inhibition we distinguish: <\/p>\n\n\n\n inhibitions. (Figure 1)<\/p>\n\n\n\n The structure of the <\/strong>inhibitor is similar to the structure of the substrate and competes with it for binding to the active centre (Figure 2).<\/p>\n\n\n\n The inhibitor is able to bind only to the free enzyme, and it can be competed out by high substrate concentration<\/strong>.<\/p>\n\n\n\n The competitive inhibitor increases the apparent Km<\/sub> value but the Vmax<\/sub> is unaltered<\/strong>.<\/p>\n\n\n\n There is no competition <\/strong>between the substrate and the inhibitor. (Figure 3)<\/p>\n\n\n\n The inhibitor usually binds at a site other than the substrate binding site<\/strong>, and its binding can not be reversed by increasing substrate concentration.<\/p>\n\n\n\n The inhibitor is able to bind both the free enzyme and the enzyme-substrate complex.<\/p>\n\n\n\n The noncompetitive inhibitor does not cause any change in KM<\/sub>, but it decreases the apparent value of Vmax<\/sub><\/strong>.<\/p>\n\n\n\n The inhibitor can not bind to the free enzyme, only to the enzyme-substrate complex, <\/strong>preventing the product formation.<\/p>\n\n\n\n It is often found in multi-substrate reactions.<\/p>\n\n\n\n Both the KM<\/sub>, and Vmax<\/sub> are altered<\/strong>. (Figure 4)<\/p>\n\n\n\n <\/p>\n<\/span>Types of inhibition<\/h2>\n<\/span>\n\n\n
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<\/a>Reversible – Competitive inhibition <\/h2>\n<\/span>\n\n\n
<\/a>Reversible – Non-Competitive inhibition<\/h2>\n<\/span>\n\n\n
<\/a>Reversible – Uncompetitive inhibition<\/h2>\n<\/span>\n\n\n
<\/a>