Nucleophile

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Virgil Hélaine - One of the best experts on this subject based on the ideXlab platform.

  • 2 deoxyribose 5 phosphate aldolase a remarkably tolerant aldolase towards Nucleophile substrates
    Chemical Communications, 2019
    Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil Hélaine
    Abstract:

    We explored a collection of 2-deoxyribose-5-phosphate aldolases (DERAs) from biodiversity for their Nucleophile substrate promiscuity. The DERAs were screened using as Nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate aldolase, the only previously known aldolase with a large Nucleophile tolerance.

  • 2 deoxyribose 5 phosphate aldolase a remarkably tolerant aldolase towards Nucleophile substrates
    Chemical Communications, 2019
    Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil Hélaine
    Abstract:

    We explored a collection of 2-deoxyribose-5-phosphate aldolases (DERAs) from biodiversity for their Nucleophile substrate promiscuity. The DERAs were screened using as Nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate aldolase, the only previously known aldolase with a large Nucleophile tolerance.

  • Breaking the Dogma of Aldolase Specificity: Simple Aliphatic Ketones and Aldehydes are Nucleophiles for Fructose-6-phosphate Aldolase
    Chemistry - A European Journal, 2017
    Co-Authors: Raquel Roldán, Virgil Hélaine, Marielle Lemaire, Israel Sanchez-moreno, Thomas Scheidt, Teodor Parella, Pere Clapés, Wolf-dieter Fessner, Christine Guérard-hélaine
    Abstract:

    D-Fructose-6-phosphate aldolase (FSA) was probed for extended Nucleophile promiscuity by using a series of fluorogenic substrates to reveal retro-aldol activity. Four Nucleophiles ethanal, propanone, butanone, and cyclopentanone were subsequently confirmed to be non-natural substrates in the synthesis direction using the wild-type enzyme and its D6H variant. This exceptional widening of the Nucleophile substrate scope offers a rapid entry, in good yields and high stereoselectivity, to less oxygenated alkyl ketones and aldehydes, which was hitherto impossible.

Domitille Chambre - One of the best experts on this subject based on the ideXlab platform.

  • 2 deoxyribose 5 phosphate aldolase a remarkably tolerant aldolase towards Nucleophile substrates
    Chemical Communications, 2019
    Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil Hélaine
    Abstract:

    We explored a collection of 2-deoxyribose-5-phosphate aldolases (DERAs) from biodiversity for their Nucleophile substrate promiscuity. The DERAs were screened using as Nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate aldolase, the only previously known aldolase with a large Nucleophile tolerance.

  • 2 deoxyribose 5 phosphate aldolase a remarkably tolerant aldolase towards Nucleophile substrates
    Chemical Communications, 2019
    Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil Hélaine
    Abstract:

    We explored a collection of 2-deoxyribose-5-phosphate aldolases (DERAs) from biodiversity for their Nucleophile substrate promiscuity. The DERAs were screened using as Nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate aldolase, the only previously known aldolase with a large Nucleophile tolerance.

Marielle Lemaire - One of the best experts on this subject based on the ideXlab platform.

  • 2 deoxyribose 5 phosphate aldolase a remarkably tolerant aldolase towards Nucleophile substrates
    Chemical Communications, 2019
    Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil Hélaine
    Abstract:

    We explored a collection of 2-deoxyribose-5-phosphate aldolases (DERAs) from biodiversity for their Nucleophile substrate promiscuity. The DERAs were screened using as Nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate aldolase, the only previously known aldolase with a large Nucleophile tolerance.

  • 2 deoxyribose 5 phosphate aldolase a remarkably tolerant aldolase towards Nucleophile substrates
    Chemical Communications, 2019
    Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil Hélaine
    Abstract:

    We explored a collection of 2-deoxyribose-5-phosphate aldolases (DERAs) from biodiversity for their Nucleophile substrate promiscuity. The DERAs were screened using as Nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate aldolase, the only previously known aldolase with a large Nucleophile tolerance.

  • Breaking the Dogma of Aldolase Specificity: Simple Aliphatic Ketones and Aldehydes are Nucleophiles for Fructose-6-phosphate Aldolase
    Chemistry - A European Journal, 2017
    Co-Authors: Raquel Roldán, Virgil Hélaine, Marielle Lemaire, Israel Sanchez-moreno, Thomas Scheidt, Teodor Parella, Pere Clapés, Wolf-dieter Fessner, Christine Guérard-hélaine
    Abstract:

    D-Fructose-6-phosphate aldolase (FSA) was probed for extended Nucleophile promiscuity by using a series of fluorogenic substrates to reveal retro-aldol activity. Four Nucleophiles ethanal, propanone, butanone, and cyclopentanone were subsequently confirmed to be non-natural substrates in the synthesis direction using the wild-type enzyme and its D6H variant. This exceptional widening of the Nucleophile substrate scope offers a rapid entry, in good yields and high stereoselectivity, to less oxygenated alkyl ketones and aldehydes, which was hitherto impossible.

Véronique De Berardinis - One of the best experts on this subject based on the ideXlab platform.

  • 2 deoxyribose 5 phosphate aldolase a remarkably tolerant aldolase towards Nucleophile substrates
    Chemical Communications, 2019
    Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil Hélaine
    Abstract:

    We explored a collection of 2-deoxyribose-5-phosphate aldolases (DERAs) from biodiversity for their Nucleophile substrate promiscuity. The DERAs were screened using as Nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate aldolase, the only previously known aldolase with a large Nucleophile tolerance.

  • 2 deoxyribose 5 phosphate aldolase a remarkably tolerant aldolase towards Nucleophile substrates
    Chemical Communications, 2019
    Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil Hélaine
    Abstract:

    We explored a collection of 2-deoxyribose-5-phosphate aldolases (DERAs) from biodiversity for their Nucleophile substrate promiscuity. The DERAs were screened using as Nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate aldolase, the only previously known aldolase with a large Nucleophile tolerance.

Marcel Salanoubat - One of the best experts on this subject based on the ideXlab platform.

  • 2 deoxyribose 5 phosphate aldolase a remarkably tolerant aldolase towards Nucleophile substrates
    Chemical Communications, 2019
    Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil Hélaine
    Abstract:

    We explored a collection of 2-deoxyribose-5-phosphate aldolases (DERAs) from biodiversity for their Nucleophile substrate promiscuity. The DERAs were screened using as Nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate aldolase, the only previously known aldolase with a large Nucleophile tolerance.

  • 2 deoxyribose 5 phosphate aldolase a remarkably tolerant aldolase towards Nucleophile substrates
    Chemical Communications, 2019
    Co-Authors: Domitille Chambre, Ekaterina Darii, J R Petit, Christine Guerardhelaine, Marielle Lemaire, Marcel Salanoubat, Véronique De Berardinis, Aline Mariage, Virgil Hélaine
    Abstract:

    We explored a collection of 2-deoxyribose-5-phosphate aldolases (DERAs) from biodiversity for their Nucleophile substrate promiscuity. The DERAs were screened using as Nucleophiles propanone, propanal, cyclobutanone, cyclopentanone, dihydroxyacetone, and glycolaldehyde with L-glyceraldehyde-3-phosphate as an electrophile in aldol addition. A DERA from Arthrobacter chlorophenolicus (DERAArthro) efficiently allowed the synthesis of the corresponding aldol adducts in good yields, displaying complementarity in terms of configuration and substrate specificity with fructose-6-phosphate aldolase, the only previously known aldolase with a large Nucleophile tolerance.