Final answer:
Allosteric cooperativity plays a key role in controlling multisubunit enzymes. It involves regulator molecules binding to the allosteric site of enzymes, causing conformational changes that affect substrate binding and reaction rates.
Step-by-step explanation:
Allosteric cooperativity is of great importance in the control of multisubunit enzymes. Allosteric enzymes have both a binding site for substrate binding and catalysis, as well as an allosteric site for regulating enzyme activity. When a regulator molecule binds to the allosteric site, it induces a conformational change in the enzyme, affecting substrate binding and reaction rates. This regulation can be either positive, increasing reaction rates, or negative, decreasing reaction rates.