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That helps a lot! I'm a novice learning about enzymatic synthesis. I'm not there yet, but my assumption is the target molecules (And reactants/intermediate-products) will all have specific chiralities, unlike the chemical-synthesis ones which may produce 50/50. Everything in my data structures (And the pubchem CID / ChEBI ids they reference) are chiral.
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Is it explained why, in this drawing, the right catalyst forms at a higher rate than the left? Or put another way why left/right catalyst gets formed at a higher rate than right? I’m trying to understand the why behind the amplification effect.
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All reagents are symmetric, so how do you design a reaction where you produce more left or right? So starting from purely symmetric reagents and catalysts, how do you produce asymmetry?

When the chirality of the product is an autocatalyst to its own chirality. So if your reaction starts off with a little more left than right due to molecular randomness, the left is an autocatalyst which means there is a runaway process and you end up at the end of the reaction with a lot more left than right.

If you repeat the reaction from scratch, it is random if you end up with a left product or a right product. But the product of your reaction is not a 50-50 mix left-right! I.e. you created asymmetry in your solution from purely symmetric solvents.

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