The Lock-and-key mechanism was first proposed by Emil Fischer which described as the enzymatic reactions whereby an enzyme with a single substrate binds temporarily to form a substrate complex.
The lock-and-key mechanism is usually associated with the complementary shapes of an enzyme with a single substrate, wherein the lock that is being referred to is the enzyme and the substrate is the key. One right sized substrate (key) fits into the active site (key hole) of the enzyme (lock).
The active site which is mentioned above is structurally complementary to the substrate. This is the temporary binding site on the enzymes. Just like a lock and key, the enzyme as the lock and the substrate as the key is said to fit together.
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