Question

Effector molecule binding changes the behavior of enzymes by altering the equilibrium between the tense (T) state and the relaxed (R) state. Effectors are classified as either homotropic or heterotropic. Match each description with homotropic effectors, heterotropic effectors, or both. Some statements may not describe either type of effector.
Homotropic effector Heterotropic effector Both an enzyme's substrate alters the K of an enzyme works by altering the T/R ratio accounts for the sigmoidal nature of a velocity versus substrate concentration curve alters the V. of an enzyme

Answer 1

Answer:

Explanation:

Homotropic effector-

• $\text{accounts for the sigmoidal nature of a velocity versus substrate concentration curve}$
• $\text{An enzyme's substrate.}$

Both -

• $\text{Works by altering T/R ratio.}$

The phrase  $\text{"accounts for the sigmoidal nature of a velocity versus }$

is relevant and can be applied for homotropic effector molecules since the heterotropic effector molecules have the possibility and affinity to change the sigmoidal curve to a more potential hyperbolic curve contingent upon the allosteric effector to be positive or negative modulator.

The expression isn't relevant for both homotropic and heterotrophic effectors since the two of them can tie to the allosteric site of allosteric enzymatic compounds.

The phrase $\text{"works by altering the T/R ratio"}$ is significant and can be applied for both homotropic and heterotropic effectors.

The expression $\text{"an enzyme's substrate"}$ is significant and applied for homotropic effectors just as when substrate molecules tie to the allosteric site of enzyme then it is regarded as homotropic effectors. The heterotropic effectors are effectors apart from substrate molecules.

The phrase $\text{"alters the} \ K_m \ \text{ of an enzyme"}$ is not applied and insignificant to none of the heterotropic or homotropic effector molecules since $K_m$ is significant for the enzymes that obey the Michaelis-Menten equation, but allosteric enzymes do not obey the Michaelis-Menten equation. Homotropic and heterotropic effectors are viable and efficient for allosteric enzymatic chemicals that don't contain