INDUCED FIT MECHANISM OF ENZYME ACTION
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This model was proposed by Koshland in 1958.
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This is a more realistic and acceptable model for enzyme-substrate complex formation.
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According to this model, the active site is not rigid and pre-shaped.
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The interaction of the enzyme with the substrate induces a fit or a conformational change in the active site of the enzyme.
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Induced fit is possible because of the flexibility of the protein molecule.
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Further, due to induced fit, the appropriate amino acids of the enzymes get repositioned to form the active site and bring about catalysis.
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There are sufficient experimental evidences from X-ray diffraction studies to prove the induced fit model.
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Koshland’s model also explains the action of allosteric modulators and competitive inhibition of the enzymes.