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Laurence Hecquet - One of the best experts on this subject based on the ideXlab platform.

  • d -Serine as a Key Building Block: Enzymatic Process Development and Smart Applications within the Cascade Enzymatic Concept
    Organic Process Research and Development, 2020
    Co-Authors: Nazim Ocal, Franck Charmantray, Mélanie L’enfant, Loredano Pollegioni, Juliette Martin, Pascal Auffray, Jérôme Collin, Laurence Hecquet
    Abstract:

    An efficient enzymatic way catalyzed by an enzyme from D-Threonine Aldolase family was developed for D-serine production at industrial scale. This process was applied to the synthesis of two valuable Ketoses, L-erythrulose and D-fructose, within cascade enzymatic concept involving both other enzymes. Indeed, D-serine was used as a substrate of D-amino acid oxidase for the in situ generation of the corresponding ketoacid, hydroxypyruvate, a key donor substrate of Transketolase. This enzyme catalyzed the irreversible transfer of the ketol group from hydroxypyruvate to an aldehyde acceptor to form a (3S)-Ketose by stereoselective carbon-carbon bond formation. The compatibility of all enzymes and substrates allowed to develop a three step enzymatic process avoiding the purification of intermediates. This strategy was validated with two TK aldehyde substrates to finally obtain the corresponding (3S)-Ketoses with a high control of the stereoselectivity and excellent aldehyde conversion rates.

Hirotsugu Hiramatsu - One of the best experts on this subject based on the ideXlab platform.

Nazim Ocal - One of the best experts on this subject based on the ideXlab platform.

  • d -Serine as a Key Building Block: Enzymatic Process Development and Smart Applications within the Cascade Enzymatic Concept
    Organic Process Research and Development, 2020
    Co-Authors: Nazim Ocal, Franck Charmantray, Mélanie L’enfant, Loredano Pollegioni, Juliette Martin, Pascal Auffray, Jérôme Collin, Laurence Hecquet
    Abstract:

    An efficient enzymatic way catalyzed by an enzyme from D-Threonine Aldolase family was developed for D-serine production at industrial scale. This process was applied to the synthesis of two valuable Ketoses, L-erythrulose and D-fructose, within cascade enzymatic concept involving both other enzymes. Indeed, D-serine was used as a substrate of D-amino acid oxidase for the in situ generation of the corresponding ketoacid, hydroxypyruvate, a key donor substrate of Transketolase. This enzyme catalyzed the irreversible transfer of the ketol group from hydroxypyruvate to an aldehyde acceptor to form a (3S)-Ketose by stereoselective carbon-carbon bond formation. The compatibility of all enzymes and substrates allowed to develop a three step enzymatic process avoiding the purification of intermediates. This strategy was validated with two TK aldehyde substrates to finally obtain the corresponding (3S)-Ketoses with a high control of the stereoselectivity and excellent aldehyde conversion rates.

Franck Charmantray - One of the best experts on this subject based on the ideXlab platform.

  • d -Serine as a Key Building Block: Enzymatic Process Development and Smart Applications within the Cascade Enzymatic Concept
    Organic Process Research and Development, 2020
    Co-Authors: Nazim Ocal, Franck Charmantray, Mélanie L’enfant, Loredano Pollegioni, Juliette Martin, Pascal Auffray, Jérôme Collin, Laurence Hecquet
    Abstract:

    An efficient enzymatic way catalyzed by an enzyme from D-Threonine Aldolase family was developed for D-serine production at industrial scale. This process was applied to the synthesis of two valuable Ketoses, L-erythrulose and D-fructose, within cascade enzymatic concept involving both other enzymes. Indeed, D-serine was used as a substrate of D-amino acid oxidase for the in situ generation of the corresponding ketoacid, hydroxypyruvate, a key donor substrate of Transketolase. This enzyme catalyzed the irreversible transfer of the ketol group from hydroxypyruvate to an aldehyde acceptor to form a (3S)-Ketose by stereoselective carbon-carbon bond formation. The compatibility of all enzymes and substrates allowed to develop a three step enzymatic process avoiding the purification of intermediates. This strategy was validated with two TK aldehyde substrates to finally obtain the corresponding (3S)-Ketoses with a high control of the stereoselectivity and excellent aldehyde conversion rates.

  • Synthesis of specially designed probes to broaden transketolase scope
    ChemCatChem, 2013
    Co-Authors: Grégory Simon, T. Eljezi, Bertrand Legeret, Franck Charmantray, José A. Castillo, Christine Guérard-hélaine, Marielle Lemaire, M. Bouzon, Philippe Marlière, Virgil Hélaine
    Abstract:

    Efficient, biocompatible, stereospecific strategies were developed to prepare eight probes to assay transketolase (TK) variants with new substrate specificities. The structure of these probes combines a sugar moiety (D-threo or L-erythro Ketose, or D-threo aldose) with the side chain of an amino acid (Ala, Leu, Val, Met, Thr) for in vivo detection of new TK activities using amino acid auxotrophs. To obtain D-threo Ketose probes, biocatalysts, such as transketolase and fructose-6-phosphate aldolase Ala129Ser, were used whereas L-erythro Ketoses and D-threo aldose probes were synthesized by the way of organocatalysis or Sharpless dihydroxylation as sustainable alternative key steps to biocatalysis.

Szu Hua Chen - One of the best experts on this subject based on the ideXlab platform.

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