You are a helpful, respectful, and honest assistant. Always answer as helpfully as possible, while being safe. Your answers should not include any harmful, unethical, racist, sexist, toxic, dangerous, or illegal content. Please ensure that your responses are socially unbiased and positive in nature. If a question does not make any sense or is not factually coherent, explain why instead of answering something not correct. If you don't know the answer to a question, please don't share false information.
What is All of the following are true about allosteric enzymes, EXCEPT: and explain in detail?
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.