How do inhibitors change the rate of enzyme controlled reaction?

 Inhibitors reduces the rate of enzyme controlled reactions.

They do so two mechanisms competitive inhibition and non-competitive inhibition

Competitive inhibition

–         Substance inhibitors’ which are structurally similar to the substrate compete with the substrate for the active                 site on the enzyme.

–         This result in fewer enzyme-substrate complex formation and therefore the rate of reaction reduces.

–         This type of inhibition is reversible.

Non- competitive inhibitions.

–         Substance (inhibitors) bearing no structural resemblance to the substrate bind with the enzymes or it cannot                 be released from it.

–         This types of inhibitions can be reversible or irreversible.

Note: in competitive inhibition, an increase in substrate concentration increases the rate of the reaction. This is because the chances of the substrate molecules binding to the active site are then higher.

However, in non-competitive inhibition, increasing the substrate concentration has no effect on the rate of reaction since the inhibitors does not bind to the active site. The degree of inhibition only depends on the concentration of the inhibitor.

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