A water molecule in the stereospecificity pocket of Candida antarctica lipase B enhances the enantioselectivity towards 2-pentanol
International audience The effect of water activity on enzyme catalyzed enantioselective transesterification was studied using a solid/gas reactor. The experimental results were compared with predictions from molecular modelling. The system studied was esterification of 2-pentanol with methyl propan...
Main Authors: | , , , , |
---|---|
Other Authors: | , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
HAL CCSD
2007
|
Subjects: | |
Online Access: | https://hal.science/hal-00329736 https://hal.science/hal-00329736/document https://hal.science/hal-00329736/file/publiaw.pdf |
id |
ftinsu:oai:HAL:hal-00329736v1 |
---|---|
record_format |
openpolar |
spelling |
ftinsu:oai:HAL:hal-00329736v1 2023-05-15T13:55:07+02:00 A water molecule in the stereospecificity pocket of Candida antarctica lipase B enhances the enantioselectivity towards 2-pentanol Léonard, Valérie Fransson, Linda Lamare, Sylvain Hult, Karl Graber, Marianne LIttoral ENvironnement et Sociétés - UMR 7266 (LIENSs) Institut national des sciences de l'Univers (INSU - CNRS)-La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) Department of Biochemistry- KTH Royal Institute of Technology Stockholm (KTH ) 2007-04-16 https://hal.science/hal-00329736 https://hal.science/hal-00329736/document https://hal.science/hal-00329736/file/publiaw.pdf en eng HAL CCSD Wiley-VCH Verlag hal-00329736 https://hal.science/hal-00329736 https://hal.science/hal-00329736/document https://hal.science/hal-00329736/file/publiaw.pdf info:eu-repo/semantics/OpenAccess ISSN: 1439-4227 EISSN: 1439-7633 ChemBioChem https://hal.science/hal-00329736 ChemBioChem, 2007, 8, pp.662-667 [SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology info:eu-repo/semantics/article Journal articles 2007 ftinsu 2023-02-08T18:03:27Z International audience The effect of water activity on enzyme catalyzed enantioselective transesterification was studied using a solid/gas reactor. The experimental results were compared with predictions from molecular modelling. The system studied was esterification of 2-pentanol with methyl propanoate as acyl donor and lipase B from Candida antarctica as catalyst. Experimental data showed a pronounced water activity effect on both reaction rate and enantioselectivity. The enantioselectivity increased from 100 at water activity close to 0 to reach a maximum of 320 at water activity 0.2. Molecular modelling revealed how a water molecule could bind in the active site and obstruct the binding of the slow reacting enantiomer. Measurements of enantioselectivity at different water activity and temperature showed that the water molecule had a high affinity to the stereospecificity pocket of the active site with a binding energy of 9 kJ mol-1 and lost all its degrees of rotation, corresponding to an entropic energy of 37 J mol-1 K-1. Article in Journal/Newspaper Antarc* Antarctica Institut national des sciences de l'Univers: HAL-INSU |
institution |
Open Polar |
collection |
Institut national des sciences de l'Univers: HAL-INSU |
op_collection_id |
ftinsu |
language |
English |
topic |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
spellingShingle |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology Léonard, Valérie Fransson, Linda Lamare, Sylvain Hult, Karl Graber, Marianne A water molecule in the stereospecificity pocket of Candida antarctica lipase B enhances the enantioselectivity towards 2-pentanol |
topic_facet |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
description |
International audience The effect of water activity on enzyme catalyzed enantioselective transesterification was studied using a solid/gas reactor. The experimental results were compared with predictions from molecular modelling. The system studied was esterification of 2-pentanol with methyl propanoate as acyl donor and lipase B from Candida antarctica as catalyst. Experimental data showed a pronounced water activity effect on both reaction rate and enantioselectivity. The enantioselectivity increased from 100 at water activity close to 0 to reach a maximum of 320 at water activity 0.2. Molecular modelling revealed how a water molecule could bind in the active site and obstruct the binding of the slow reacting enantiomer. Measurements of enantioselectivity at different water activity and temperature showed that the water molecule had a high affinity to the stereospecificity pocket of the active site with a binding energy of 9 kJ mol-1 and lost all its degrees of rotation, corresponding to an entropic energy of 37 J mol-1 K-1. |
author2 |
LIttoral ENvironnement et Sociétés - UMR 7266 (LIENSs) Institut national des sciences de l'Univers (INSU - CNRS)-La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) Department of Biochemistry- KTH Royal Institute of Technology Stockholm (KTH ) |
format |
Article in Journal/Newspaper |
author |
Léonard, Valérie Fransson, Linda Lamare, Sylvain Hult, Karl Graber, Marianne |
author_facet |
Léonard, Valérie Fransson, Linda Lamare, Sylvain Hult, Karl Graber, Marianne |
author_sort |
Léonard, Valérie |
title |
A water molecule in the stereospecificity pocket of Candida antarctica lipase B enhances the enantioselectivity towards 2-pentanol |
title_short |
A water molecule in the stereospecificity pocket of Candida antarctica lipase B enhances the enantioselectivity towards 2-pentanol |
title_full |
A water molecule in the stereospecificity pocket of Candida antarctica lipase B enhances the enantioselectivity towards 2-pentanol |
title_fullStr |
A water molecule in the stereospecificity pocket of Candida antarctica lipase B enhances the enantioselectivity towards 2-pentanol |
title_full_unstemmed |
A water molecule in the stereospecificity pocket of Candida antarctica lipase B enhances the enantioselectivity towards 2-pentanol |
title_sort |
water molecule in the stereospecificity pocket of candida antarctica lipase b enhances the enantioselectivity towards 2-pentanol |
publisher |
HAL CCSD |
publishDate |
2007 |
url |
https://hal.science/hal-00329736 https://hal.science/hal-00329736/document https://hal.science/hal-00329736/file/publiaw.pdf |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1439-4227 EISSN: 1439-7633 ChemBioChem https://hal.science/hal-00329736 ChemBioChem, 2007, 8, pp.662-667 |
op_relation |
hal-00329736 https://hal.science/hal-00329736 https://hal.science/hal-00329736/document https://hal.science/hal-00329736/file/publiaw.pdf |
op_rights |
info:eu-repo/semantics/OpenAccess |
_version_ |
1766261353839853568 |