The powerful enzyme urease instantly catalyzes the rapid hydrolysis of urea completely into and , but entirely and flawlessly fails to catalyze the virtually identical hydrolysis of -methyl urea. Whic

Question

The powerful enzyme urease instantly catalyzes the rapid hydrolysis of urea completely into $CO_2$ and $NH_3$, but entirely and flawlessly fails to catalyze the virtually identical hydrolysis of $N$ -methyl urea. Which specific core biochemical principle best and fully explains this striking observation?

Prashant Kotian · Accepted Answer

Correct answer: B. Enzymes are unbelievably structurally specific to their targeted substrates. Urease accommodates only urea into its highly rigid, perfectly shaped active site exactly as a specific key operates a specific lock. The minor addition of a sterically bulky methyl group physically blocks the molecule from securely entering the catalytic active site.

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