If the activation energy is lowered, bond strength has decreased. How does purely orientating the reactants closer to one another lower the activation energy in a protein? The only thing I can think of is steric strain.

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    $\begingroup$ IMO how enzymes work, ie how do they bring about phenomenal rate enhancements at RT, is one of the great unanswered questions in biochemistry. However, for a great attempt at explaining why, see how do enzymes work by Joseph Kraut $\endgroup$ – user1136 Dec 7 '18 at 15:15
  • $\begingroup$ We welcome new posts to SE Biology, but ask that posters read the advice in the help about posting questions. Your question has problems which can be solved by clearly setting out your assumptions and their basis. You state "if activation energy is lowered bond strength is decreased". You do not say what bonds you are talking about (the transition state?) and your basis for this assumption. Then you say "how does purely orientating…" without saying that you have read (where?) that this is how enzymes works. Please revise carefully. $\endgroup$ – David Dec 7 '18 at 16:05

The activation energy is not only lowered by orientating the substrate but by stabilizing the transition state.

According to the induced fit model many enzymes show a higher binding affinity to the transition state of a substrate.

  • $\begingroup$ We welcome new participants to SE Biology, but this is a question and answer site, not a discussion site, so what we expect from an answer is more than the two lines here. First, you need to consider whether this question should be answered at all. It is so poorly constructed that I would say no. However if you must, you need to clarify the question and the false assumptions, porvide more detail, and provide external justification for your answer. Without links or references, how can anyone tell whether or not you are correct? $\endgroup$ – David Dec 7 '18 at 16:09

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