<prompt> All of the following are true about allosteric enzymes, EXCEPT:Allosteric enzymes cant have structure beyond the teiary structureAllosteric enzymes have a regulatory site other than the active siteAllosteric enzymes do not show Michaelis-Menten kineticsAllosteric modulators bind noncovalently to allosteric site  <response>: Be Aware that Question is asking about the wrongfalse statement: Allosteric enzymes also contain a site other than active site which binds to allosteric regulator. Allosteric enzymes dont follow Michaelis-Menten kinetics. They do obey Hills 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. 