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The active site of an enzyme is the binding site where catalysis occurs. The structure and chemical properties of the active site allow the recognition and binding of the substrate.

The active site is usually a small pocket at the surface of the enzyme that contains residues responsible for the susbtrate specificity (charge, hydrophobicity, steric hindrance) and catalytic residues which often act as proton donors or acceptors or are responsible for binding a cofactor such as Pyridoxal, Thiamine or NAD.

Main article - See Enzyme catalysis

The active site is also the site of inhibition of enzymes (see Enzyme inhibitor article).


There are several models of how enzymes work: the lock-and-key model and the induced fit model. Substrates bind to the active site of the enzyme or a specificity pocket through hydrogen bonds, hydrophobic interactions, temporary covalent bond or a combination of all of these. Residues of the active site will act as donors or acceptors of protons or other groups on the substrate to facilitate the reaction. In other words, the active site modifies the reaction mechanism in order to decrease the activation energy of the reaction. The product is usually unstable in the active site due to steric hindrances that force it to be released and return the enzyme to its initial state.

See also[]

  • Catalytic triad
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