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3. Tuning of Pectin Methylesterification: PECTIN METHYLESTERASE INHIBITOR 7 MODULATES THE PROCESSIVE ACTIVITY OF CO-EXPRESSED PECTIN METHYLESTERASE 3 IN A pH-DEPENDENT MANNER

Author

Sénéchal, Fabien, L'Enfant, Mélanie, Domon, Jean-Marc, Rosiau, Emeline, Crépeau, Marie-Jeanne, Surcouf, Ogier, Esquivel-Rodriguez, Juan, Marcelo, Paulo, Mareck, Alain, Guérineau, François, Kim, Hyung-Rae, Mravec, Jozef, Bonnin, Estelle, Jamet, Elisabeth, Kihara, Daisuke, Lerouge, Patrice, Ralet, Marie-Christine, Pelloux, Jérôme, and Rayon, Catherine

Published
2015
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8. One‐Pot Cascade Synthesis of (3S)‐Hydroxyketones Catalyzed by Transketolase via Hydroxypyruvate Generated in Situ from d‐Serine by d‐Amino Acid Oxidase.

Author

L'enfant, Mélanie, Bruna, Felipe, Lorillière, Marion, Ocal, Nazim, Fessner, Wolf‐Dieter, Pollegioni, Loredano, Charmantray, Franck, and Hecquet, Laurence

Subjects
*AMINO acid oxidase, *TRANSKETOLASE, *GEOBACILLUS stearothermophilus, *CARBON-carbon bonds, *CHEMICAL synthesis, *ESCHERICHIA coli
Abstract

We described an efficient in situ generation of hydroxypyruvate from d‐serine catalyzed by a d‐amino acid oxidase from Rhodotorula gracilis. This strategy revealed an interesting alternative to the conventional chemical synthesis of hydroxypyruvate starting from toxic bromopyruvate or to the enzymatic transamination from l‐serine requiring an additional substrate as amino acceptor. Hydroxypyruvate thus produced was used as donor substrate of transketolases from Escherichia coli or from Geobacillus stearothermophilus catalyzing the stereoselective formation of a carbon−carbon bond. The enzymatic cascade reaction was performed in one‐pot in the presence of d‐serine and appropriate aldehydes for the synthesis of valuable (3S)‐hydroxyketones, which were obtained with high enantio‐ and diastereoselectivity and in good yield. The efficiency of the process was based on the irreversibility of both reactions allowing complete conversion of d‐serine and aldehydes. [ABSTRACT FROM AUTHOR]

Published
2019
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9. Biochemical characterization of an Arabidopsis pectin methylesterase AtPME3 and a pectin methylesterase inhibitor

Author

Sénéchal, Fabien, L’Enfant, Mélanie, Domon, Jean-Marc, Surcouf, Ogier, Quéméner, Bernard, Esquivel-Rodriguez, Juan, Mareck, Alain, Guérineau, François, Kim, Hyung-Rae, Bonnin, Estelle, Jamet, Elisabeth, Kihara, Daisuke, Ralet, Marie-Christine, Lerouge, Patrice, Pelloux, Jérôme, Rayon, Catherine, Biologie des Plantes et Innovation (BIOPI), Université de Picardie Jules Verne (UPJV), Laboratoire de Glycobiologie et Matrice Extracellulaire Végétale (Glyco-MEV), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Laboratoire de Recherche en Sciences Végétales (LRSV), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Biologie des Plantes et Innovation - UR UPJV 3900 (BIOPI), Dynamique et Evolution des Parois cellulaires végétales, Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Université de Picardie Jules Verne (UPJV)-Transfrontalière BioEcoAgro - UMR 1158 (BioEcoAgro), Université d'Artois (UA)-Université de Liège-Université de Picardie Jules Verne (UPJV)-Université du Littoral Côte d'Opale (ULCO)-Université de Lille-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-JUNIA (JUNIA), Université catholique de Lille (UCL)-Université catholique de Lille (UCL)-Université d'Artois (UA)-Université de Liège-Université du Littoral Côte d'Opale (ULCO)-Université de Lille-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-JUNIA (JUNIA), Université catholique de Lille (UCL)-Université catholique de Lille (UCL), Department of Biological Sciences [Lafayette IN], Purdue University [West Lafayette], Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), and Institut National de Recherche Agronomique (INRA). UR Biopolymères, Interactions Assemblages (1268)

Subjects
[SDV.BIO]Life Sciences [q-bio]/Biotechnology, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], [SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacy, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], [SDV.BV.AP]Life Sciences [q-bio]/Vegetal Biology/Plant breeding, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], [SDV.IDA]Life Sciences [q-bio]/Food engineering, [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], [SDV.BDD]Life Sciences [q-bio]/Development Biology, ComputingMilieux_MISCELLANEOUS
Abstract

Brevet : P2-43; International audience; Pectin methylesterase (PME) catalyses the de-methylesterification of pectin in plant cell walls during cell elongation. While it is generally assumed that fungal PMEs have a random mode of action, plant PMEs are thought to act in a processive manner to generate long stretches of non-methylesterified residues. However, it is unlikely that all plant PMEs have a strictly similar mode of action. One A. thalianaPME gene (PME3) has been over-expressed in an heterologous system and its protein product purified by affinity chromatography. Homogalacturonans (HGs) from citrus pectin with varied degrees of methyl esterification (DM) have been generated and characterized. Kinetic properties of PME3 have been determined. PME activity from the purified PME3 was performed on the characterized HG substrates with respect to pH. PME3 shows a highest activity at a basic pH but displays different affinities towards specific methyl esterification patterns on the pectin substrates. Demethylesterified blocks assessed by measuring the degree of blockiness and absolute degree of blockiness will be presented. PME activities are also regulated by endogenous pectin methylesterase inhibitors (PMEIs), which control the DM of HG. PMEI7 inhibits PME3 enzyme activity. Docking analysis indicates that the inhibition of PME3 occurs via the PMEI7 interaction with a PME ligand-binding cleft structure.

Published
2013

10. Biochemical characterization of an Arabidopsis pectin methylesterase AtPME3 and a pectin methylesterase inhibitor

Author

Fabien Senechal, Enfant, Mélanie L., Jean-Marc Domon, Ogier Surcouf, Bernard Quemener, Juan Esquivel-Rodríguez, Alain Mareck, François Guerineau, Hyung-Rae Kim, Estelle Bonnin, Jamet, E., Jozef Mravec, Kihara, D., Marie-Christine Ralet, Lerouge, P., Jérome Pelloux, Catherine Rayon, Biologie des Plantes et Innovation - UR UPJV 3900 (BIOPI), Université de Picardie Jules Verne (UPJV), UFR des Sciences et Techniques Mont-Saint-Aignan, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Department of Biological Sciences [Lafayette IN], Purdue University [West Lafayette], Laboratoire de Glycobiologie et Matrice Extracellulaire Végétale (Glyco-MEV), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Dynamique et Evolution des Parois cellulaires végétales, Laboratoire de Recherche en Sciences Végétales (LRSV), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Department of Plant and Environmental Sciences, department of Plant, and Institut National de Recherche Agronomique (INRA). UR Biopolymères, Interactions Assemblages (1268).

Subjects
[SDV.IDA]Life Sciences [q-bio]/Food engineering, food and beverages
Abstract

National audience; Pectin methylesterase (PME) catalyses the de-methylesterification of pectin in plant cell walls during cell elongation. While it is generally assumed that fungal PMEs have a random mode of action, plant PMEs are thought to act in a processive manner to generate long stretches of non-methylesterified residues. However, it is unlikely that all plant PMEs have a strictly similar mode of action. One A. thalianaPME gene (PME3) has been over-expressed in an heterologous system and its protein product purified by affinity chromatography. Homogalacturonans (HGs) from citrus pectin with varied degrees of methyl esterification (DM) have been generated and characterized. Kinetic properties of PME3 have been determined. PME activity from the purified PME3 was performed on the characterized HG substrates with respect to pH. PME3 shows a highest activity at a basic pH but displays different affinities towards specific methyl esterification patterns on the pectin substrates. Demethylesterified blocks assessed by measuring the degree of blockiness and absolute degree of blockiness will be presented. PME activities are also regulated by endogenous pectin methylesterase inhibitors (PMEIs), which control the DM of HG. PMEI7 inhibits PME3 enzyme activity. Docking analysis indicates that the inhibition of PME3 occurs via the PMEI7 interaction with a PME ligand-binding cleft structure.

Published
2013

11. Tuning of pectin methylesterification:pectin methylesterase inhibitor 7 modulates the processive activity of co-expressed pectin methylesterase 3 in a pH-dependent manner

Author

Sénéchal, Fabien, L'Enfant, Mélanie, Domon, Jean-Marc, Rosiau, Emeline, Crépeau, Marie-Jeanne, Surcouf, Ogier, Esquivel-Rodriguez, Juan, Marcelo, Paulo, Mareck, Alain, Guérineau, François, Kim, Hyung-Rae, Mravec, Jozef, Bonnin, Estelle, Jamet, Elisabeth, Kihara, Daisuke, Lerouge, Patrice, Ralet, Marie-Christine, Pelloux, Jérôme, Rayon, Catherine, Sénéchal, Fabien, L'Enfant, Mélanie, Domon, Jean-Marc, Rosiau, Emeline, Crépeau, Marie-Jeanne, Surcouf, Ogier, Esquivel-Rodriguez, Juan, Marcelo, Paulo, Mareck, Alain, Guérineau, François, Kim, Hyung-Rae, Mravec, Jozef, Bonnin, Estelle, Jamet, Elisabeth, Kihara, Daisuke, Lerouge, Patrice, Ralet, Marie-Christine, Pelloux, Jérôme, and Rayon, Catherine

Published
2015

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