Molecular rules for selectivity in lipase-catalysed acylation of lysine
International audience The selectivity of L-lysine acylation by lauric acid catalysed by Candida antarctica lipase B (CALB) was investigated combining experimental and theoretical methodologies. Experiments showed the near-exclusive acylation of lysine ε-amino group; only traces of product resulting...
Published in: | Process Biochemistry |
---|---|
Main Authors: | , , , , , , |
Other Authors: | , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
HAL CCSD
2018
|
Subjects: | |
Online Access: | https://hal.archives-ouvertes.fr/hal-01883545 https://hal.archives-ouvertes.fr/hal-01883545/document https://hal.archives-ouvertes.fr/hal-01883545/file/Pub_CALB_Lysine_HAL.pdf https://doi.org/10.1016/j.procbio.2018.07.021 |
id |
ftccsdartic:oai:HAL:hal-01883545v1 |
---|---|
record_format |
openpolar |
spelling |
ftccsdartic:oai:HAL:hal-01883545v1 2023-05-15T13:58:43+02:00 Molecular rules for selectivity in lipase-catalysed acylation of lysine Dettori, Léna Jelsch, Christian Guiavarc’h, Yann Delaunay, Stéphane Framboisier, Xavier Chevalot, I. Humeau, Catherine Laboratoire Réactions et Génie des Procédés (LRGP) Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS) Cristallographie, Résonance Magnétique et Modélisations (CRM2) 2018-11 https://hal.archives-ouvertes.fr/hal-01883545 https://hal.archives-ouvertes.fr/hal-01883545/document https://hal.archives-ouvertes.fr/hal-01883545/file/Pub_CALB_Lysine_HAL.pdf https://doi.org/10.1016/j.procbio.2018.07.021 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2018.07.021 hal-01883545 https://hal.archives-ouvertes.fr/hal-01883545 https://hal.archives-ouvertes.fr/hal-01883545/document https://hal.archives-ouvertes.fr/hal-01883545/file/Pub_CALB_Lysine_HAL.pdf doi:10.1016/j.procbio.2018.07.021 info:eu-repo/semantics/OpenAccess ISSN: 1359-5113 Process Biochemistry https://hal.archives-ouvertes.fr/hal-01883545 Process Biochemistry, Elsevier, 2018, 74, pp.50 - 60. ⟨10.1016/j.procbio.2018.07.021⟩ selectivity molecular modelisation acylation [SDV]Life Sciences [q-bio] [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM] [SDV.BIO]Life Sciences [q-bio]/Biotechnology info:eu-repo/semantics/article Journal articles 2018 ftccsdartic https://doi.org/10.1016/j.procbio.2018.07.021 2021-11-07T01:42:35Z International audience The selectivity of L-lysine acylation by lauric acid catalysed by Candida antarctica lipase B (CALB) was investigated combining experimental and theoretical methodologies. Experiments showed the near-exclusive acylation of lysine ε-amino group; only traces of product resulting from the acylation of lysine α-amino group were observed fleetingly. Molecular modelling simulations were performed aiming to understand the molecular rules for selectivity. Flexible docking simulations combined with structural investigations into lysine/CALB binding modes also suggested the preferential acylation of lysine ε-amino group without, however, excluding the acylation of the lysine α-amino group. Electrostatic interaction energy between lysine and the residues covering the catalytic cavity was calculated in order to understand the discrimination between the two lysine amino groups. The results suggests that the proximity of the carboxylate group hinders the binding of the substrate in configurations enabling the N-acylation. Key interactions with the polar region covering the catalytic triad were identified and a plausible explanation for selectivity was proposed. Article in Journal/Newspaper Antarc* Antarctica Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) Process Biochemistry 74 50 60 |
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 |
selectivity molecular modelisation acylation [SDV]Life Sciences [q-bio] [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM] [SDV.BIO]Life Sciences [q-bio]/Biotechnology |
spellingShingle |
selectivity molecular modelisation acylation [SDV]Life Sciences [q-bio] [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM] [SDV.BIO]Life Sciences [q-bio]/Biotechnology Dettori, Léna Jelsch, Christian Guiavarc’h, Yann Delaunay, Stéphane Framboisier, Xavier Chevalot, I. Humeau, Catherine Molecular rules for selectivity in lipase-catalysed acylation of lysine |
topic_facet |
selectivity molecular modelisation acylation [SDV]Life Sciences [q-bio] [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM] [SDV.BIO]Life Sciences [q-bio]/Biotechnology |
description |
International audience The selectivity of L-lysine acylation by lauric acid catalysed by Candida antarctica lipase B (CALB) was investigated combining experimental and theoretical methodologies. Experiments showed the near-exclusive acylation of lysine ε-amino group; only traces of product resulting from the acylation of lysine α-amino group were observed fleetingly. Molecular modelling simulations were performed aiming to understand the molecular rules for selectivity. Flexible docking simulations combined with structural investigations into lysine/CALB binding modes also suggested the preferential acylation of lysine ε-amino group without, however, excluding the acylation of the lysine α-amino group. Electrostatic interaction energy between lysine and the residues covering the catalytic cavity was calculated in order to understand the discrimination between the two lysine amino groups. The results suggests that the proximity of the carboxylate group hinders the binding of the substrate in configurations enabling the N-acylation. Key interactions with the polar region covering the catalytic triad were identified and a plausible explanation for selectivity was proposed. |
author2 |
Laboratoire Réactions et Génie des Procédés (LRGP) Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS) Cristallographie, Résonance Magnétique et Modélisations (CRM2) |
format |
Article in Journal/Newspaper |
author |
Dettori, Léna Jelsch, Christian Guiavarc’h, Yann Delaunay, Stéphane Framboisier, Xavier Chevalot, I. Humeau, Catherine |
author_facet |
Dettori, Léna Jelsch, Christian Guiavarc’h, Yann Delaunay, Stéphane Framboisier, Xavier Chevalot, I. Humeau, Catherine |
author_sort |
Dettori, Léna |
title |
Molecular rules for selectivity in lipase-catalysed acylation of lysine |
title_short |
Molecular rules for selectivity in lipase-catalysed acylation of lysine |
title_full |
Molecular rules for selectivity in lipase-catalysed acylation of lysine |
title_fullStr |
Molecular rules for selectivity in lipase-catalysed acylation of lysine |
title_full_unstemmed |
Molecular rules for selectivity in lipase-catalysed acylation of lysine |
title_sort |
molecular rules for selectivity in lipase-catalysed acylation of lysine |
publisher |
HAL CCSD |
publishDate |
2018 |
url |
https://hal.archives-ouvertes.fr/hal-01883545 https://hal.archives-ouvertes.fr/hal-01883545/document https://hal.archives-ouvertes.fr/hal-01883545/file/Pub_CALB_Lysine_HAL.pdf https://doi.org/10.1016/j.procbio.2018.07.021 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1359-5113 Process Biochemistry https://hal.archives-ouvertes.fr/hal-01883545 Process Biochemistry, Elsevier, 2018, 74, pp.50 - 60. ⟨10.1016/j.procbio.2018.07.021⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2018.07.021 hal-01883545 https://hal.archives-ouvertes.fr/hal-01883545 https://hal.archives-ouvertes.fr/hal-01883545/document https://hal.archives-ouvertes.fr/hal-01883545/file/Pub_CALB_Lysine_HAL.pdf doi:10.1016/j.procbio.2018.07.021 |
op_rights |
info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.1016/j.procbio.2018.07.021 |
container_title |
Process Biochemistry |
container_volume |
74 |
container_start_page |
50 |
op_container_end_page |
60 |
_version_ |
1766267062091513856 |