This is a real-world medical entrance exam question, please give the true answer based on the question and selection. Topic name: Enzyme kinetics, Subject name: Biochemistry
All of the following are true about allosteric enzymes, EXCEPT: 
Select and explain. 
A. Allosteric enzymes can't have structure beyond the teiary structure, B. Allosteric enzymes have a regulatory site other than the active site, C. Allosteric enzymes do not show Michaelis-Menten kinetics, D. Allosteric modulators bind noncovalently to allosteric site
A: Allosteric enzymes can't have structure beyond the teiary structure
Answer: A: Allosteric enzymes can't have structure beyond the teiary structure 
Explanation: 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.