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- W3138913650 abstract "Abstract A two‐enzyme cascade reaction plus in situ oxidative decarboxylation for the transformation of readily available canonical and non‐canonical l ‐α‐amino acids into 2‐substituted 3‐hydroxycarboxylic acid derivatives is described. The biocatalytic cascade consisted of an oxidative deamination of l ‐α‐amino acids by an l ‐α‐amino acid deaminase from Cosenzaea myxofaciens , rendering 2‐oxoacid intermediates, with an ensuing aldol addition reaction to formaldehyde, catalyzed by metal‐dependent ( R )‐ or ( S )‐selective carboligases namely 2‐oxo‐3‐deoxy‐ l ‐rhamnonate aldolase (YfaU) and ketopantoate hydroxymethyltransferase (KPHMT), respectively, furnishing 3‐substituted 4‐hydroxy‐2‐oxoacids. The overall substrate conversion was optimized by balancing biocatalyst loading and amino acid and formaldehyde concentrations, yielding 36–98% aldol adduct formation and 91–98% ee for each enantiomer. Subsequent in situ follow‐up chemistry via hydrogen peroxide‐driven oxidative decarboxylation afforded the corresponding 2‐substituted 3‐hydroxycarboxylic acid derivatives. magnified image" @default.
- W3138913650 created "2021-03-29" @default.
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- W3138913650 date "2021-03-31" @default.
- W3138913650 modified "2023-10-03" @default.
- W3138913650 title "Chemoenzymatic Production of Enantiocomplementary 2‐Substituted 3‐Hydroxycarboxylic Acids from <scp>l</scp> ‐α‐Amino Acids" @default.
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- W3138913650 doi "https://doi.org/10.1002/adsc.202100145" @default.
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