There are four different types of specificity: Absolute, group, linkage, stereo chemical specificity. The ‘Lock and Key’ concept of protein-ligand binding has dominated descriptions of these interactions, and has been effectively translated to computational molecular docking approaches.
They are either loosely or firmly bound.Įnzyme specificity is the ability of an enzyme to discriminate among competing substrates for it. Activators are inorganic ions working as cofactors. Prosthetic group is a metal ion or an organic compound that is covalently bound to an enzyme required for its activity. Coenzyme is a loosely bound organic cofactor that is required for enzyme activity. Lower the activation energy, faster is the rate.Ĭofactor of an enzyme is the non-protein component and is essential for its catalytic activity. Enzymes work by lowering the activation energy. As per induced fit hypothesis, active site expands and contracts on substrate interaction.Īctivation energy is the amount of energy required to convert all the reacting substances from ground state to transition state. In lock and key hypothesis, enzyme holds the substrate as a lock holding the key. Several steps of enzyme action results in the formation of products and eventually the enzyme is regenerated. Reaction catalysis and product formation occurs at catalytic site of the enzyme. Substrate is held by weak interactions at the binding site of the enzyme. A Peptide bond is formed by amino acid condensation. The active site is the location on the surface of the enzyme where the catalysis of chemical reaction takes place. The substrate binds with the enzyme’s active site and the enzyme catalyzes the chemical reaction involving the substrate.
Audiobooks for 40+ Courses in Science and Math (Lite Edition)Īn enzyme is a protein that catalyzes a chemical reaction and a substrate is a molecule which is acted upon by an enzyme.
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