Which one of the following statements regarding allosteric enzymes is correct?

Allosteric enzymes are complex regulatory proteins that do not follow standard Michaelis-Menten kinetics [4]. Unlike typical enzymes that exhibit a hyperbolic velocity versus substrate concentration graph, allosteric enzymes display a sigmoidal (S-shaped) curve [1]. This sigmoidal behavior is a hallmark of cooperativity, where the binding of a ligand at one site influences the binding at others [3]. Structurally, these enzymes are typically multisubunit (oligomeric) proteins [2]. Each subunit generally contains a catalytic site (active site) and at least one distinct regulatory site (allosteric site) [3]. The binding of an effector molecule to the regulatory site induces conformational changes that either increase or decrease the enzyme's affinity for the substrate at the active site, allowing for precise metabolic control [4].

Sources

1. [1] https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/allosteric-enzyme
2. [4] https://www.nature.com/articles/s41586-024-07813-2
3. [3] https://www.sciencedirect.com/science/article/abs/pii/S0045206811000897
4. [2] https://pmc.ncbi.nlm.nih.gov/articles/PMC2575317/