The essential difference between denaturation and inhibition of an enzyme is that denaturation
- A. always occurs at the active site only
- B. can be reversed by adding more substrate
- C. involves the loss of the enzyme's three dimensional shape and is usually permanent
- D. increases the rate of the reaction
Explanation
Denaturation unfolds the whole protein, so the enzyme is destroyed as a catalyst and no amount of substrate will restore it, whereas most inhibition leaves the enzyme intact and is reversible when the inhibitor is removed or, for competitive inhibitors, outcompeted. High temperature and extreme pH denature, while specific molecules inhibit. Only competitive inhibition is relieved by extra substrate.
Related questions
Above its optimum temperature the rate of an enzyme catalysed reaction falls sharply because the enzyme
Which enzyme works at an optimum pH of about 2?
At a constant enzyme concentration, increasing substrate concentration eventually stops increasing the reaction rate because
Between 0 degrees Celsius and the optimum, a rise of 10 degrees roughly doubles the rate of an enzyme catalysed reaction because
The optimum temperature of most human enzymes is about