Hydrophobic pocket engineering of arylmalonate decarboxylase expands its substrate scope towards the synthesis of the (R)-enantiomers of sterically hindered carboxylic acids
Chem. Commun., 2026, Accepted Manuscript DOI: 10.1039/D6CC02837C, Communication
Elske van der Pol, Lisa-Marie Krammer, Johannes Eder, Dominik Gross, Roland C. Fischer, Kenji Miyamoto, Robert Kourist, Rolf Breinbauer Arylmalonate decarboxylase (AMDase) stereoselectively converts disubstituted malonates to chiral carboxylic acids, but its substrate spectrum is very limited regarding the size of the smaller substituent. Inspired by the observation that...
