Regulation of enzyme activity by allosteric effectors
A) can only increase enzyme activity.
B) can only decrease activity.
C) usually involves monomeric enzymes.
D) involves an equilibrium between two conformational forms of an enzyme.
E) requires covalent attachment of the effector to the enzyme.

Question

Quizplus · Accepted Answer

Allosteric effectors can either increase or decrease enzyme activity by inducing a conformational change in the enzyme's structure. This involves an equilibrium between two conformational forms of the enzyme, referred to as the R (relaxed) and T (tense) states. When an allosteric effector binds to the enzyme, it can shift the equilibrium towards the R or T state, resulting in an increase or decrease in enzyme activity, respectively. Allosteric regulation typically involves oligomeric enzymes consisting of multiple subunits that can interact with each other to affect enzyme activity. Covalent attachment of effectors to the enzyme is not required for allosteric regulation.

Regulation of Enzyme Activity by Allosteric Effectors