allosteric enzymes:a.exhibit michaelis-menten kinetics.b.are never regulated by substrate binding.c.have their activity changed by changes in intersubunit interactions.d.always have both inhibitory and activating modulators.

Respuesta :

The activity of allosteric enzymes can change due to variations in intersubunit interactions.

Multiple protein subunits are typically present in allosteric enzymes. Effectors are ligands that bind to allosteric enzymes and change binding at a different site on the enzyme. When a substrate also functions as an effector and affects the binding of additional substrate molecules, this is known as homotropic regulation.

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