Is the Michaelis-Menten equation useful when studying allosteric enzymes?

a) Yes Only if the enzyme displays positive cooperativity.

b) Only if the enzyme displays negative cooperativity. No

Question

Josue Hess

Biology

31 March, 13:18

Is the Michaelis-Menten equation useful when studying allosteric enzymes?

a) Yes Only if the enzyme displays positive cooperativity.

b) Only if the enzyme displays negative cooperativity. No

+1

Answers (1)

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Ainsley Anthony · Answer 1

b) Only if the enzyme displays negative cooperativity. No

Explanation:

Allosteric enzymes have more than one active site and have positive co-operativity. They yield a sigmoidal curve (Rate of reaction versus substrate) while those enzymes which follow the Michaelis-Menten equation yield a rectangular hyperbolic curve.

Is the Michaelis-Menten equation useful when studying allosteric enzymes?a) Yes Only if the enzyme displays positive cooperativity.b) Only if the enzyme displays negative cooperativity. No

Is the Michaelis-Menten equation useful when studying allosteric enzymes?

a) Yes Only if the enzyme displays positive cooperativity.

b) Only if the enzyme displays negative cooperativity. No