How does the lock and key model of enzymes action explain the highly specific way some enzymes select a substrate?

Answer 1

This refers to the hypothesis proposed by Emil Fischer in 1894 but confirmed until the 20th century. Fischer proposed that the specificity of an enzyme (the lock) for its substrate (the key) arises from their geometrically complementary shapes. More specifically, the noncovalent forces through which substrates and other molecules bind to the enzyme are identical in character to the forces that dictate the conformations of the proteins themselves. Both involve van der Waals, electrostatic, hydrogen bonding, and hydrophobic interactions.

A substrate-binding site consists of an interaction or cleft on the surface of an enzyme molecule that is complementary in shape to the surface (geometrical complementarity). Molecules that differ in shape of functional group distribution from the substrate cannot productively bind to the enzyme; that is, they cannot form enzyme-substrate complexes that lead to the formation of products.

Answer 2

The lock and key model explains that enzymes have specific active sites that only fit the shape of particular substrates, like a key fitting into a lock. This specific molecular complementarity allows enzymes to catalyze reactions selectively by only binding to their specific substrate, ensuring efficiency and accuracy in biochemical reactions.