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