Question 1
Q1A biochemist is studying a novel enzyme that displays cooperative binding kinetics. The reaction velocity is measured at various substrate concentrations, yielding a sigmoidal curve on a Michaelis-Menten plot. Which of the following structural features is most likely responsible for this observed cooperativity?
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Correct answer: C
Cooperative binding, characterized by a sigmoidal kinetic curve, is a hallmark of allosteric enzymes that are typically composed of multiple subunits (a multimeric structure). The binding of a substrate molecule to one active site induces a conformational change in the enzyme that is transmitted to the other subunits, altering their affinity for the substrate. This communication between subunits is the basis of cooperativity. A single active site cannot exhibit cooperativity. Non-competitive inhibitors affect Vmax but do not induce the characteristic sigmoidal curve of positive cooperativity. Covalent modification is a form of regulation but is not the direct structural cause of cooperativity itself.