Convergent in situ Generation of Both Transketolase Substrates via Transaminase and Aldolase Reactions for Sequential One‐Pot, Three‐Step Cascade Synthesis of Ketoses
| Autor: | Marion Lorillière, Laurence Hecquet, Wolf-Dieter Fessner, Pere Clapés, Christine Guérard-Hélaine, Franck Charmantray, Thierry Gefflaut |
|---|---|
| Přispěvatelé: | Institut de Chimie de Clermont-Ferrand (ICCF), SIGMA Clermont (SIGMA Clermont)-Institut de Chimie du CNRS (INC)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020])-Centre National de la Recherche Scientifique (CNRS), Technische Universität Darmstadt (TU Darmstadt), Institute for Advanced Chemistry-CSIC Barcelona, Technische Universität Darmstadt - Technical University of Darmstadt (TU Darmstadt) |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
Glycolaldehyde biology 010405 organic chemistry Transamination Organic Chemistry Aldolase A Substrate (chemistry) Transketolase 010402 general chemistry 01 natural sciences Combinatorial chemistry Catalysis 0104 chemical sciences Inorganic Chemistry chemistry.chemical_compound chemistry Nucleophile Cascade reaction Biocatalysis biology.protein [CHIM]Chemical Sciences Physical and Theoretical Chemistry |
| Zdroj: | ChemCatChem ChemCatChem, Wiley, 2020, 12 (3), pp.812-817. ⟨10.1002/cctc.201901756⟩ ChemCatChem, 2020, 12 (3), pp.812-817. ⟨10.1002/cctc.201901756⟩ Digital.CSIC. Repositorio Institucional del CSIC instname |
| ISSN: | 1867-3899 |
| DOI: | 10.1002/cctc.201901756⟩ |
| Popis: | International audience; We describe an efficient three‐enzyme, sequential one‐pot cascade reaction where both transketolase substrates are generated in situ in a convergent fashion. The nucleophilic donor substrate hydroxypyruvate was obtained from l‐serine and pyruvate by a transaminase‐catalyzed reaction. In parallel, three different (2S)‐α‐hydroxylated aldehydes, l‐glyceraldehyde, d‐threose, and l‐erythrose, were generated as electrophilic acceptors from simple achiral compounds glycolaldehyde and formaldehyde by d‐fructose‐6‐phosphate aldolase catalysis. The compatibility of the three enzymes was studied in terms of temperature, enzyme ratio and substrate concentration. The efficiency of the process relied on the irreversibility of the transketolase reaction, driving a shift of the reversible transamination reaction and securing the complete conversion of all substrates. Three valuable (3S,4S)‐ketoses, l‐ribulose, d‐tagatose, and l‐psicose were obtained in good yields with high diastereoselectivity. |
| Databáze: | OpenAIRE |
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