Convergent in situ Generation of Both Transketolase Substrates via Transaminase and Aldolase Reactions for Sequential One‐Pot, Three‐Step Cascade Synthesis of Ketoses
| العنوان: | Convergent in situ Generation of Both Transketolase Substrates via Transaminase and Aldolase Reactions for Sequential One‐Pot, Three‐Step Cascade Synthesis of Ketoses |
|---|---|
| المؤلفون: | Marion Lorillière, Laurence Hecquet, Wolf-Dieter Fessner, Pere Clapés, Christine Guérard-Hélaine, Franck Charmantray, Thierry Gefflaut |
| المساهمون: | 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) |
| المصدر: | 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 |
| بيانات النشر: | HAL CCSD, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | 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 |
| الوصف: | 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. |
| اللغة: | English |
| تدمد: | 1867-3899 |
| DOI: | 10.1002/cctc.201901756⟩ |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::937909a3b48328dbabf3143197c8921e https://hal.archives-ouvertes.fr/hal-02991624 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....937909a3b48328dbabf3143197c8921e |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 18673899 |
|---|---|
| DOI: | 10.1002/cctc.201901756⟩ |