{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pickl M"],"funding":["Austrian Science Fund FWF"],"pagination":["2866-2876"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7611260"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["363(11)"],"pubmed_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-hydroxy-carboxylic 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 <i>Cosenzaea myxofaciens</i>, rendering 2-oxoacid intermediates, with an ensuing aldol addition reaction to formaldehyde, catalyzed by metal-dependent (<i>R</i>)- or (<i>S</i>)-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."],"journal":["Advanced synthesis & catalysis"],"pubmed_title":["Chemoenzymatic Production of Enantiocomplementary 2-Substituted 3-Hydroxycarboxylic Acids from L-α-Amino Acids."],"pmcid":["PMC7611260"],"funding_grant_id":["J 4242","J 4242-B21"],"pubmed_authors":["Joglar J","Clapes P","Pickl M","Marin-Valls R","Bujons J"],"additional_accession":[]},"is_claimable":false,"name":"Chemoenzymatic Production of Enantiocomplementary 2-Substituted 3-Hydroxycarboxylic Acids from L-α-Amino Acids.","description":"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-hydroxy-carboxylic 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 <i>Cosenzaea myxofaciens</i>, rendering 2-oxoacid intermediates, with an ensuing aldol addition reaction to formaldehyde, catalyzed by metal-dependent (<i>R</i>)- or (<i>S</i>)-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.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jun","modification":"2024-11-20T12:00:10.424Z","creation":"2022-02-10T20:42:11.169Z"},"accession":"S-EPMC7611260","cross_references":{"pubmed":["34276272"],"doi":["10.1002/adsc.202100145"]}}