this post was submitted on 08 Aug 2023
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It has to to with the LDF repulsion and attraction. The study stated it was a 4D aspect of the CYP450s. It alters the active site to bind to different substrates depending on the toxins found in the liver.
Thanks for the explanation, but I still don't quite see how this is special, afaik LDF is analogous to van der Waals force? Is this basically the same as a "loose" active site? (Ie. Can bind a range of similar substrates) Is it because the LDF force acts on an allosteric site of the enzyme and thus changes the active site? I also don't understand their use of the term "4D". (Sorry for being difficult, just trying to understand the significance of the paper)
Van der Waals is the attraction aspect of LDF, while steric repulsion is the flipside and still a part of LDF interactions. But based on the possible substrates LDF interaction with CYP450, the active site + mechanism of action will adjust to work with what's around. Not just an allosteric aspect where a select few molecules can fit in the active site. Or at least that's my understanding of the study's findings.
Edit: The 4D aspect is referencing the LDF impact on the enzymes shape and function. LDF impacts all biochem reactions, dipole and hydrophobic forces are a bigger aspect to substrate binding though. But this breaks the mold of what we thought we knew about enzymes and opens the door for a more indepth understanding of biochemical reactions.
I see, thanks for the explanations :)