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  Enzyme Action

Enzyme Action:

The molecular events which accompany the conversion of substrate in products constitute the method of enzyme action. Enzyme action on its substrate affects either in the formation of chemical bonds or degradation of chemical bonds in the substrate molecules.

ES Complex Formation:

As per to Michaelis – Menton theory, the enzyme E joints with the substrate S to create an intermediate enzyme substrate complex ES. After that this complex splits into product P and enzyme E is regenerated. The enzyme can once again combine along with the fresh molecule of the substrate in identical manner. The creation of enzyme substrate complex like an intermediate throughout the reaction has been proved through spectroscopic studies. Thus, a simple enzymatic reaction might be written as

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In which E, S and P stand for enzyme, substrate and product correspondingly. ES and EP are complexes of the enzyme along with substrate and product correspondingly. At the end of the reaction together with the needed products the enzyme is reproduced in its original form and can include in another round of catalysis. ES complex is an extremely energised, transiently available complex that can be easily degraded to make the product.

In the creation of enzyme substrate complexes, the substrate molecules attach at fixed particular sites on the enzyme molecules. These particular points on enzyme molecules in which the substrate molecules attach are termed as active site /catalytic site.

Active sites on the enzymes are generally given by fixed functional group of amino acids available in the enzyme protein. For instance, free hydroxyl group of serine, sulfhydryl group of cysteine, phenolic group of tyrosine, and imidazolyl group of histidine are some of the significant catalytic groups exist in enzyme active sites.

 

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