In the book Lehninger Principles of Biochemistry, there is a metal stick analogy to explain why an enzyme being compliment to its substrate would actually make a terrible enzyme.
If the enzyme is complimentary to the substrate, it will form many weak interactions, hence the enzyme-substrate (ES) complex is very stable, meaning it will require more energy to reach the transition state, so very few products are made
If the enzyme isn't entirely compliment to its substrate, it will form a few weak interactions (that allows it to bind to its substrate). This isn't its lowest energy state, as there are still more weak interactions that can occur. The weak interactions will mould the substrate into its transition state. This would mean that the transition state is the most stable state in this environment (I would assume). The thing that I am confused about is that if the transition state would be the most stable state, then why would it go on to form a product? Once the weak interactions mould the substrate, then energy would be released from the substrate, forming a transition state, therefore making the transition state have lower energy than the substrate, not higher, so the reaction profile in the final diagram doesn't really make sense to me. Is there anything that I am missing or not understanding?
I would really appreciate someone clearing up any confusion about this. Thanks.
