Emil Fischer was the first to describe the Lock-and-Key mechanism, which involves an enzyme momentarily binding to one substrate to generate a substrate complex.
The locking mechanism and key are frequently connected with complementary enzyme forms that share a single substrate, with the enzyme serving as the lock and the substrate serving as the key. One substrate (key) fits perfectly into the enzyme’s active site (keyhole) (lock).
The above-mentioned active site is physically compatible with the substrate. This is the enzymes’ temporary binding site. The enzyme, like a lock and a key, is said to fit the lock and the substrate together.

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