A molecular modelling study to rationalize the regioselectivity in acylation of flavonoïd glycosides catalysed by Candida antartica lipase B
International audience The regioselective behaviour of the Candida antarctica lipase B (CALB) towards two flavonoid glycosides, rutin and isoquercitrin, in the acetylation reaction was investigated through molecular modelling. A protocol constituted by a Monte Carlo-based docking procedure and class...
Published in: | Journal of Molecular Catalysis B: Enzymatic |
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ftccsdartic:oai:HAL:inria-00435075v1 2023-05-15T13:57:43+02:00 A molecular modelling study to rationalize the regioselectivity in acylation of flavonoïd glycosides catalysed by Candida antartica lipase B De Oliveira, Eduardo Humeau, Catherine Chebil, Latifa Maia, Elaine Dehez, François Maigret, Bernard Ghoul, Mohamed Engasser, Jean-Marc Ecole Nationale Supérieure d'Agronomie et des Industries Alimentaires (ENSAIA) Université de Lorraine (UL) Centre de Recherches sur les Macromolécules Végétales (CERMAV) Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF) Knowledge representation, reasonning (ORPAILLEUR) INRIA Lorraine Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria)-Laboratoire Lorrain de Recherche en Informatique et ses Applications (LORIA) Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique de Lorraine (INPL)-Université Nancy 2-Université Henri Poincaré - Nancy 1 (UHP)-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique de Lorraine (INPL)-Université Nancy 2-Université Henri Poincaré - Nancy 1 (UHP) 2009 https://hal.inria.fr/inria-00435075 https://doi.org/10.1016/j.molcatb.2009.01.011 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2009.01.011 inria-00435075 https://hal.inria.fr/inria-00435075 doi:10.1016/j.molcatb.2009.01.011 ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.inria.fr/inria-00435075 Journal of Molecular Catalysis B: Enzymatic, Elsevier, 2009, 59 (1-3), pp.96-105. ⟨10.1016/j.molcatb.2009.01.011⟩ Candida antarctica lipase B Docking Flavonoid acylation Molecular modelling Regioselectivity [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology info:eu-repo/semantics/article Journal articles 2009 ftccsdartic https://doi.org/10.1016/j.molcatb.2009.01.011 2021-12-05T03:50:04Z International audience The regioselective behaviour of the Candida antarctica lipase B (CALB) towards two flavonoid glycosides, rutin and isoquercitrin, in the acetylation reaction was investigated through molecular modelling. A protocol constituted by a Monte Carlo-based docking procedure and classical force fields calculations was applied to find probable binding modes of the substrates inside the catalytic cavity and optimize the corresponding complexes. The analysis of these complexes allowed identifying productive ones (that means, those able to lead to the formation of the ester product) according to three parameters: (1) protein distortion; (2) stability of hydrogen bond interactions with the oxyanion hole residues; (3) localization of hydroxyl groups with regard to the region comprised between the catalytic histidine and serine residues. Results showed that the aglycon part of both rutin and isoquercitrin was localized at the entrance of the binding pocket, stabilized by hydrogen bond and hydrophobic interactions. The sugar part of the flavonoidswas placed close to the pocket bottom. In particular, only the primary 6" -OH of the isoquercitrin glucose and the secondary 4'" -OH of the rutin rhamnosewere expected to be acetylated, as theywere the only ones to stabilize simultaneously near to the catalytic histidine and the acetate bound to the catalytic serine. These findings are in accordance with experimental data and give a suitable explanation, at an atomic level, of the regioselectivity of CALB in the flavonoid glycosides acetylation. Article in Journal/Newspaper Antarc* Antarctica antartic* Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) Journal of Molecular Catalysis B: Enzymatic 59 1-3 96 105 |
institution |
Open Polar |
collection |
Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
op_collection_id |
ftccsdartic |
language |
English |
topic |
Candida antarctica lipase B Docking Flavonoid acylation Molecular modelling Regioselectivity [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
spellingShingle |
Candida antarctica lipase B Docking Flavonoid acylation Molecular modelling Regioselectivity [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology De Oliveira, Eduardo Humeau, Catherine Chebil, Latifa Maia, Elaine Dehez, François Maigret, Bernard Ghoul, Mohamed Engasser, Jean-Marc A molecular modelling study to rationalize the regioselectivity in acylation of flavonoïd glycosides catalysed by Candida antartica lipase B |
topic_facet |
Candida antarctica lipase B Docking Flavonoid acylation Molecular modelling Regioselectivity [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
description |
International audience The regioselective behaviour of the Candida antarctica lipase B (CALB) towards two flavonoid glycosides, rutin and isoquercitrin, in the acetylation reaction was investigated through molecular modelling. A protocol constituted by a Monte Carlo-based docking procedure and classical force fields calculations was applied to find probable binding modes of the substrates inside the catalytic cavity and optimize the corresponding complexes. The analysis of these complexes allowed identifying productive ones (that means, those able to lead to the formation of the ester product) according to three parameters: (1) protein distortion; (2) stability of hydrogen bond interactions with the oxyanion hole residues; (3) localization of hydroxyl groups with regard to the region comprised between the catalytic histidine and serine residues. Results showed that the aglycon part of both rutin and isoquercitrin was localized at the entrance of the binding pocket, stabilized by hydrogen bond and hydrophobic interactions. The sugar part of the flavonoidswas placed close to the pocket bottom. In particular, only the primary 6" -OH of the isoquercitrin glucose and the secondary 4'" -OH of the rutin rhamnosewere expected to be acetylated, as theywere the only ones to stabilize simultaneously near to the catalytic histidine and the acetate bound to the catalytic serine. These findings are in accordance with experimental data and give a suitable explanation, at an atomic level, of the regioselectivity of CALB in the flavonoid glycosides acetylation. |
author2 |
Ecole Nationale Supérieure d'Agronomie et des Industries Alimentaires (ENSAIA) Université de Lorraine (UL) Centre de Recherches sur les Macromolécules Végétales (CERMAV) Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF) Knowledge representation, reasonning (ORPAILLEUR) INRIA Lorraine Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria)-Laboratoire Lorrain de Recherche en Informatique et ses Applications (LORIA) Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique de Lorraine (INPL)-Université Nancy 2-Université Henri Poincaré - Nancy 1 (UHP)-Institut National de Recherche en Informatique et en Automatique (Inria)-Centre National de la Recherche Scientifique (CNRS)-Institut National Polytechnique de Lorraine (INPL)-Université Nancy 2-Université Henri Poincaré - Nancy 1 (UHP) |
format |
Article in Journal/Newspaper |
author |
De Oliveira, Eduardo Humeau, Catherine Chebil, Latifa Maia, Elaine Dehez, François Maigret, Bernard Ghoul, Mohamed Engasser, Jean-Marc |
author_facet |
De Oliveira, Eduardo Humeau, Catherine Chebil, Latifa Maia, Elaine Dehez, François Maigret, Bernard Ghoul, Mohamed Engasser, Jean-Marc |
author_sort |
De Oliveira, Eduardo |
title |
A molecular modelling study to rationalize the regioselectivity in acylation of flavonoïd glycosides catalysed by Candida antartica lipase B |
title_short |
A molecular modelling study to rationalize the regioselectivity in acylation of flavonoïd glycosides catalysed by Candida antartica lipase B |
title_full |
A molecular modelling study to rationalize the regioselectivity in acylation of flavonoïd glycosides catalysed by Candida antartica lipase B |
title_fullStr |
A molecular modelling study to rationalize the regioselectivity in acylation of flavonoïd glycosides catalysed by Candida antartica lipase B |
title_full_unstemmed |
A molecular modelling study to rationalize the regioselectivity in acylation of flavonoïd glycosides catalysed by Candida antartica lipase B |
title_sort |
molecular modelling study to rationalize the regioselectivity in acylation of flavonoïd glycosides catalysed by candida antartica lipase b |
publisher |
HAL CCSD |
publishDate |
2009 |
url |
https://hal.inria.fr/inria-00435075 https://doi.org/10.1016/j.molcatb.2009.01.011 |
genre |
Antarc* Antarctica antartic* |
genre_facet |
Antarc* Antarctica antartic* |
op_source |
ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.inria.fr/inria-00435075 Journal of Molecular Catalysis B: Enzymatic, Elsevier, 2009, 59 (1-3), pp.96-105. ⟨10.1016/j.molcatb.2009.01.011⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2009.01.011 inria-00435075 https://hal.inria.fr/inria-00435075 doi:10.1016/j.molcatb.2009.01.011 |
op_doi |
https://doi.org/10.1016/j.molcatb.2009.01.011 |
container_title |
Journal of Molecular Catalysis B: Enzymatic |
container_volume |
59 |
container_issue |
1-3 |
container_start_page |
96 |
op_container_end_page |
105 |
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