Hydrophobic pocket engineering of arylmalonate decarboxylase expands its substrate scope towards the synthesis of the (R)-enantiomers of sterically hindered carboxylic acids
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Hydrophobic pocket engineering of arylmalonate decarboxylase expands its substrate scope towards the synthesis of the (R)-enantiomers of sterically hindered carboxylic acids
van der Pol, E.; Krammer, L.-M.; Eder, J.; Gross, D.; Fischer, R.; Miyamoto, K.; Breinbauer, R.; Kourist, R.
AbstractArylmalonate 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 (S)-selective AMDase variants also convert larger substrates, we unlocked the synthesis of the (R)-enantiomers of alpha-aryl and alpha-alkenyl n-butanoic and n-pentanoic acids, respectively, in exquisite enantiopurity