- #1
shredder666
- 63
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I've always wondered how enzymes could tell the difference between too much substrate and too little substrate to initiate allosteric activities, my teacher tells me that its kinda like collision theory in chemical bonding. That would make sense because if there's too much product, then some of it has got to bind with the allosteric site in the last enzyme. But then what if there's like 1 product in 100 gizzilion substrates that gets binded into the allosteric site? Does that mean even in "normal" enzyme activity, some enzymes are in the "work faster" mode and some enzymes are in the "work at normal rate" mode?