Thermodynamic analysis of enzyme enantioselectivity: a statistical approach by means of new differential HybridMIF descriptors
The study of relationships between substrate structure and enzyme stereoselectivity was approached by means of a new molecular descriptor: the “differential Hybrid Molecular Interaction Field” (dH-MIF). The descriptor was conceived with the purpose of combining enthalpic and entropic information rel...
Published in: | Biocatalysis and Biotransformation |
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Online Access: | http://hdl.handle.net/11368/2744901 https://doi.org/10.3109/10242422.2013.838025 |
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ftunitriestiris:oai:arts.units.it:11368/2744901 2023-05-15T14:13:51+02:00 Thermodynamic analysis of enzyme enantioselectivity: a statistical approach by means of new differential HybridMIF descriptors FERRARIO, VALERIO EBERT, CYNTHIA GARDOSSI, Lucia Foscato M. Ferrario, Valerio Foscato, M. Ebert, Cynthia Gardossi, Lucia 2013 STAMPA http://hdl.handle.net/11368/2744901 https://doi.org/10.3109/10242422.2013.838025 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000325814900006 volume:31, 2013 firstpage:272 lastpage:280 numberofpages:9 journal:BIOCATALYSIS AND BIOTRANSFORMATION http://hdl.handle.net/11368/2744901 doi:10.3109/10242422.2013.838025 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84885931718 enantioselettivity entropy lipase computational chemistry GRID molecular descriptors info:eu-repo/semantics/article 2013 ftunitriestiris https://doi.org/10.3109/10242422.2013.838025 2023-04-09T06:12:10Z The study of relationships between substrate structure and enzyme stereoselectivity was approached by means of a new molecular descriptor: the “differential Hybrid Molecular Interaction Field” (dH-MIF). The descriptor was conceived with the purpose of combining enthalpic and entropic information related to enzyme–enantiomer interactions. The dH-MIFs were developed based on experimental data previously published by the group of Karl Hult on the enantioselectivity of the W104A mutant of lipase B from Candida antarctica, which is endowed with an enlarged stereoselectivity pocket. Because of the increased conformational freedom of substrates, the entropic contribution to enantiodiscrimination is particularly relevant in kinetic resolution of alcohols catalyzed by this enzyme. By combining molecular dynamic simulations and GRID analysis the new dH-MIF descriptors proved to be able to extract both enthalpic and entropic information from models of the tetrahedral intermediates of enantiomers. Article in Journal/Newspaper Antarc* Antarctica Università degli studi di Trieste: ArTS (Archivio della ricerca di Trieste) Hult ENVELOPE(-13.688,-13.688,65.101,65.101) Biocatalysis and Biotransformation 31 5 272 280 |
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Open Polar |
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Università degli studi di Trieste: ArTS (Archivio della ricerca di Trieste) |
op_collection_id |
ftunitriestiris |
language |
English |
topic |
enantioselettivity entropy lipase computational chemistry GRID molecular descriptors |
spellingShingle |
enantioselettivity entropy lipase computational chemistry GRID molecular descriptors FERRARIO, VALERIO EBERT, CYNTHIA GARDOSSI, Lucia Foscato M. Thermodynamic analysis of enzyme enantioselectivity: a statistical approach by means of new differential HybridMIF descriptors |
topic_facet |
enantioselettivity entropy lipase computational chemistry GRID molecular descriptors |
description |
The study of relationships between substrate structure and enzyme stereoselectivity was approached by means of a new molecular descriptor: the “differential Hybrid Molecular Interaction Field” (dH-MIF). The descriptor was conceived with the purpose of combining enthalpic and entropic information related to enzyme–enantiomer interactions. The dH-MIFs were developed based on experimental data previously published by the group of Karl Hult on the enantioselectivity of the W104A mutant of lipase B from Candida antarctica, which is endowed with an enlarged stereoselectivity pocket. Because of the increased conformational freedom of substrates, the entropic contribution to enantiodiscrimination is particularly relevant in kinetic resolution of alcohols catalyzed by this enzyme. By combining molecular dynamic simulations and GRID analysis the new dH-MIF descriptors proved to be able to extract both enthalpic and entropic information from models of the tetrahedral intermediates of enantiomers. |
author2 |
Ferrario, Valerio Foscato, M. Ebert, Cynthia Gardossi, Lucia |
format |
Article in Journal/Newspaper |
author |
FERRARIO, VALERIO EBERT, CYNTHIA GARDOSSI, Lucia Foscato M. |
author_facet |
FERRARIO, VALERIO EBERT, CYNTHIA GARDOSSI, Lucia Foscato M. |
author_sort |
FERRARIO, VALERIO |
title |
Thermodynamic analysis of enzyme enantioselectivity: a statistical approach by means of new differential HybridMIF descriptors |
title_short |
Thermodynamic analysis of enzyme enantioselectivity: a statistical approach by means of new differential HybridMIF descriptors |
title_full |
Thermodynamic analysis of enzyme enantioselectivity: a statistical approach by means of new differential HybridMIF descriptors |
title_fullStr |
Thermodynamic analysis of enzyme enantioselectivity: a statistical approach by means of new differential HybridMIF descriptors |
title_full_unstemmed |
Thermodynamic analysis of enzyme enantioselectivity: a statistical approach by means of new differential HybridMIF descriptors |
title_sort |
thermodynamic analysis of enzyme enantioselectivity: a statistical approach by means of new differential hybridmif descriptors |
publishDate |
2013 |
url |
http://hdl.handle.net/11368/2744901 https://doi.org/10.3109/10242422.2013.838025 |
long_lat |
ENVELOPE(-13.688,-13.688,65.101,65.101) |
geographic |
Hult |
geographic_facet |
Hult |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000325814900006 volume:31, 2013 firstpage:272 lastpage:280 numberofpages:9 journal:BIOCATALYSIS AND BIOTRANSFORMATION http://hdl.handle.net/11368/2744901 doi:10.3109/10242422.2013.838025 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84885931718 |
op_doi |
https://doi.org/10.3109/10242422.2013.838025 |
container_title |
Biocatalysis and Biotransformation |
container_volume |
31 |
container_issue |
5 |
container_start_page |
272 |
op_container_end_page |
280 |
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1766286388680982528 |