5330-85-8Relevant academic research and scientific papers
Rational Engineered C-Acyltransferase Transforms Sterically Demanding Acyl Donors
??d?o-Dobrowolska, Anna,Hammerer, Lucas,Pavkov-Keller, Tea,Gruber, Karl,Kroutil, Wolfgang
, p. 1094 - 1101 (2020/01/21)
The biocatalytic Friedel-Crafts acylation has been identified recently for the acetylation of resorcinol using activated acetic acid esters for the synthesis of acetophenone derivatives catalyzed by an acyltransferase. Because the wild-type enzyme is limited to acetic and propionic derivatives as the substrate, variants were designed to extend the substrate scope of this enzyme. By rational protein engineering, the key residue in the active site was identified which can be replaced to allow binding of bulkier acyl moieties. The single-point variant F148V enabled the transformation of previously inaccessible medium chain length alkyl and alkoxyalkyl carboxylic esters as donor substrates with up to 99% conversion and up to >99% isolated yield.
