Question

Generate and analyse plots describing the kinetic properties of allosteric enzymes what happens to the Km as more ___ are introduced? - more inhibitors - more activators.

Answer 1

Allosteric enzymes can be regulated by allosteric inhibitors and activators. Allosteric inhibitors reduce substrate binding and increase Km, while allosteric activators enhance substrate binding and decrease Km.

Step-by-step explanation:

In allosteric enzymes, the substrate binding and affinity can be regulated by allosteric inhibitors and activators. Allosteric inhibitors modify the active site of the enzyme, reducing or preventing substrate binding. As a result, the Km (Michaelis-Menten constant) increases, indicating a decrease in substrate affinity. On the other hand, allosteric activators enhance substrate binding by modifying the active site, leading to a decrease in Km and an increase in substrate affinity.