Which statement most accurately explains how allosteric regulation can change an enzyme's catalytic activity? view available hint(s) which statement most accurately explains how allosteric regulation can change an enzyme's catalytic activity? in allosteric activation, a regulatory molecule binds to a location other than the active site, resulting in a change in enzyme shape that allows the active site to bind substrate. in allosteric activation, a regulatory molecule binds to the active site, allowing substrate binding. in allosteric inhibition, a regulatory molecule binds to the active site, blocking substrate binding. in allosteric inhibition, a regulatory molecule binds to a location other than the active site, resulting in a change in enzyme shape that allows the active site to bind substrate.

In allosteric inhibition, a regulatory molecule binds to a location other than the active site, resulting in a change in enzyme shape that allows the active site to bind substrate.

Explanation:

Allosteric regulation of an enzyme can be positive or negative, but it always involves effector molecules that bind to non-active site of the enzyme and change its conformation. That site of binding is called allosteric or regulatory site. If the enzyme activity is enhanced effector molecule is called allosteric activator but if the activity is decreased effector molecules are allosteric inhibitors.

the correct answer is: b. pantala flavescens, because these organisms would have a high level of genetic variation due to sexual reproduction.  

because involves two organisms (parents) whose genetic material combines, sexual reproduction leads to genetic variation in new generations of offspring. the offspring is an unique organism, with new genome, more protected with the higher ability to adapted. this process is fundamental to evolution.

answer; the above statement/question is (false);