Synthesis of γ-Hydroxy-α-amino Acid Derivatives by Enzymatic Tandem Aldol Addition-Transamination Reactions

Three enzymatic routes toward γ-hydroxy-α-amino acids by tandem aldol addition-transamination one-pot two-step reactions are reported. The approaches feature an enantioselective aldol addition of pyruvate to various nonaromatic aldehydes catalyzed by trans - o -hydroxybenzylidene pyruvate hydratase-...

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Bibliographic Details
Authors: Moreno, Carlos J., Hernández, Karel|||0000-0001-7367-4426, Charnok, Simon J., Gittings, Samantha, Bolte, Michael|||0000-0001-5296-6251, Joglar, Jesús|||0000-0002-3391-1682, Bujons, Jordi|||0000-0003-2944-2905, Parella Coll, Teodor|||0000-0002-1914-2709, Clapés, Pere|||0000-0001-5541-4794
Format: article
Publication Date:2021
Country:España
Institution:Universitat Autònoma de Barcelona
Repository:Dipòsit Digital de Documents de la UAB
Language:English
OAI Identifier:oai:ddd.uab.cat:250459
Online Access:https://ddd.uab.cat/record/250459
https://dx.doi.org/urn:doi:10.1021/acscatal.1c00210
Access Level:Open access
Keyword:Biocatalysis
2-oxoacid aldolase
Transaminases
Aldol addition
Reductive amination
Γ-hydroxy-α-amino acids
Description
Summary:Three enzymatic routes toward γ-hydroxy-α-amino acids by tandem aldol addition-transamination one-pot two-step reactions are reported. The approaches feature an enantioselective aldol addition of pyruvate to various nonaromatic aldehydes catalyzed by trans - o -hydroxybenzylidene pyruvate hydratase-aldolase (HBPA) from Pseudomonas putida. This affords chiral 4-hydroxy-2-oxo acids, which were subsequently enantioselectively aminated using S -selective transaminases. Three transamination processes were investigated involving different amine donors and transaminases: (i) -Ala as an amine donor with pyruvate recycling, (ii) a benzylamine donor using benzaldehyde lyase from Pseudomonas fluorescens Biovar I (BAL) to transform the benzaldehyde formed into benzoin, minimizing equilibrium limitations, and (iii) -Glu as an amine donor with a double cascade comprising branched-chain α-amino acid aminotransferase (BCAT) and aspartate amino transferase (AspAT), both from E. coli, using -Asp as a substrate to regenerate -Glu. The γ-hydroxy-α-amino acids thus obtained were transformed into chiral α-amino-γ-butyrolactones, structural motifs found in many biologically active compounds and valuable intermediates for the synthesis of pharmaceutical agents.