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Keywords:

  • β-hydroxy amino acids;
  • aldolases;
  • enzyme models;
  • stereoselectivity
Thumbnail image of graphical abstract

Optimizing the active site: A pyridoxal 5′-phosphate(PLP)-dependent alanine racemase was converted into a retro-aldolase by a single active-site mutation. This new catalyst reacts efficiently with quaternary β-hydroxy α-amino acids, a class of molecules that natural aldolases have not been evolved to handle. Computational docking experiments suggest a novel mechanism for this process and rationalize the stereochemical preferences of the enzyme.