All of the following are true about allosteric enzymes, EXCEPT:
Be Aware that Question is asking about the wrong/false statement: Allosteric enzymes also contain a site other than active site which binds to allosteric regulator. Allosteric enzymes don't follow Michaelis-Menten kinetics. They do obey Hill's equation. Allosteric enzymes are usually multi-subunit enzymes. Binding of allosteric regulator to the allosteric site alters the substrate affinity of active site. This is known as cooperativity.This can be either positive or negative. A multi-subunit enzyme will obviously have quaternary structure - option a is wrong.
Allosteric enzymes can't have structure beyond the teiary structure
Allosteric enzymes have a regulatory site other than the active site
Allosteric enzymes do not show Michaelis-Menten kinetics
Allosteric modulators bind noncovalently to allosteric site
Enzyme kinetics