The enzyme urease readily catalyses the hydrolysis of urea into and . However, it entirely fails to catalyse the hydrolysis of -methyl urea. Which biochemical principle best explains this observation?

Question

The enzyme urease readily catalyses the hydrolysis of urea into $CO_2$ and $NH_3$. However, it entirely fails to catalyse the hydrolysis of $N$ -methyl urea. Which biochemical principle best explains this observation?

Prashant Kotian · Accepted Answer

Correct answer: B. Enzymes are highly specific to their substrates. Urease specifically accommodates urea into its rigid active site via the "lock and key" mechanism. The additional steric bulk of the methyl group in -methyl urea prevents it from fitting into the active site, resulting in no catalytic reaction.

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