Competitive Inhibition:
Competitive inhibitors can join reversibly by the active site of enzyme and compete with the substrate for binding along with the active site. If the site is used via the inhibitor it is not available for the binding of the substrate illustrated in the below diagram. The competitive inhibitor all the time resembles the structure of the substrate. In a number of cases competitive inhibitors are exact structural analogues of the substrates. The combination of competitive inhibitor (I) along with enzyme (E) can be written in similar way as combination with substrate, even though the inhibitor cannot be chemically transformed to products.
Ki is equivalent to the dissociation constant for the enzyme – inhibitor complex EI.
The degree of inhibition relies on the comparative concentration of the substrate and the inhibitor. It as well depends upon the relative affinity of inhibitor in the direction of enzyme active site. So, via increasing the substrate concentration we can reduce the degree of inhibition keeping inhibitor concentration at constant level.
The typical instance is the inhibition of succinate dehydrogenase through malonate and other dicarboxylic acids. Succinate dehydrogenase is a member of the group of enzymes catalyzing the Krebs tricarboxylic acid cycle.
It catalyzes the exclusion of two hydrogen atoms from the succinate’s two methylene carbon atoms. Succinate dehydrogenase is inhibited via malonate that resembles succinate in comprising two ionized carboxyl groups.Several micro organisms such as bacteria synthesize the vitamin folic acid from para-aminobenzoic acid. Sulphanilamide and other sulfa drugs are structural analogs of para-aminobenzoic acid. Thus, sulfa drugs work as competitive inhibitor and take place the active site of some bacterial enzyme catalyzing this reaction. While this reaction is influenced, it blocks the folic acid biosynthesis that is necessary for the growth of micro organisms, finaly results in the death of the micro organisms. So, several sulfa drugs work as antibiotics
Diagram: Competitive inhibition
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