A: Allosteric enzymes do not show a typical M | vedclass

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(C) Assertion $(A)$ is correct: Allosteric enzymes exhibit sigmoidal kinetics rather than the hyperbolic kinetics described by the Michaelis-Menten eq

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Assertion is correct,but Reason is incorrect.

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(C) Assertion $(A)$ is correct: Allosteric enzymes exhibit sigmoidal kinetics rather than the hyperbolic kinetics described by the Michaelis-Menten equation. They do not follow standard Michaelis-Menten behavior because their activity is regulated by the binding of effectors at sites other than the active site.Reason $(R)$ is incorrect: Enzymes are highly specific and have different optimal $pH$ values depending on their structure and the environment in which they function (e.g.,pepsin works at acidic $pH$,while trypsin works at alkaline $pH$).

$A$: Allosteric enzymes do not show a typical Michaelis-Menten constant or behavior.
$R$: All enzymes work at the same $pH$.

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$A$: Allosteric enzymes do not show a typical Michaelis-Menten constant or behavior.$R$: All enzymes work at the same $pH$.