6tf8

Publication Abstract from PubMed

Controlling regio- and stereoselectivity of aldol additions is generally challenging. Here we show that an artificial aldolase with high specificity for acetone as the aldol donor can be reengineered via single active site mutations to accept linear and cyclic aliphatic ketones with notable efficiency, regioselectivity, and stereocontrol. Biochemical and crystallographic data show how the mutated residues modulate the binding and activation of specific aldol donors, as well as their subsequent reaction with diverse aldehyde acceptors. Broadening the substrate scope of this evolutionarily naive catalyst proved much easier than previous attempts to redesign natural aldolases, suggesting that such proteins may be excellent starting points for the development of customized biocatalysts for diverse practical applications.

Engineered Artificial Carboligases Facilitate Regioselective Preparation of Enantioenriched Aldol Adducts.,Macdonald DS, Garrabou X, Klaus C, Verez R, Mori T, Hilvert D J Am Chem Soc. 2020 Jun 10;142(23):10250-10254. doi: 10.1021/jacs.0c02351. Epub, 2020 May 28. PMID:32427470^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.