Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymes

The enzymatic breakdown of carbohydrates plays a critical role in several biological events and enables the development of sustainable processes to obtain bioproducts and biofuels. In this scenario, the design of efficient inhibitors for glycosidases that can act as drug targets and the engineering...

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Detalles Bibliográficos
Autores: Abrahão Bueno Morais, Mariana, Nin Hill, Alba, Rovira i Virgili, Carme
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/219212
Acceso en línea:https://hdl.handle.net/2445/219212
Access Level:acceso abierto
Palabra clave:Sucre
Dinàmica molecular
Enzims
Sugar
Molecular dynamics
Enzymes
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spelling Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymesAbrahão Bueno Morais, MarianaNin Hill, AlbaRovira i Virgili, CarmeSucreDinàmica molecularEnzimsSugarMolecular dynamicsEnzymesThe enzymatic breakdown of carbohydrates plays a critical role in several biological events and enables the development of sustainable processes to obtain bioproducts and biofuels. In this scenario, the design of efficient inhibitors for glycosidases that can act as drug targets and the engineering of carbohydrate-active enzymes with tailored catalytic properties is of remarkable importance. To guide rational approaches, it is necessary to elucidate enzyme molecular mechanisms, in particular understanding how the microenvironment modulates the conformational space explored by the substrate. Computer simulations, especially those based on ab initio methods, have provided a suitable atomic description of carbohydrate conformations and catalytic reactions in several glycosidase families. In this review, we will focus on how the active-site topology (pocket or cleft) and mode of cleavage (endo or exo) can affect the catalytic mechanisms adopted by glycosidases, in particular the substrate conformations along the reaction coordinate.Elsevier2023info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/219212Articles publicats en revistes (Química Inorgànica i Orgànica)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.1016/j.cbpa.2023.102282Current Opinion in Chemical Biology, 2023, vol. 74, p. 1-8https://doi.org/10.1016/j.cbpa.2023.102282cc-by-nc-nd (c) Abrahão Bueno Morais, Mariana, et al., 2023http://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/2192122026-05-27T06:46:51Z
dc.title.none.fl_str_mv Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymes
title Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymes
spellingShingle Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymes
Abrahão Bueno Morais, Mariana
Sucre
Dinàmica molecular
Enzims
Sugar
Molecular dynamics
Enzymes
title_short Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymes
title_full Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymes
title_fullStr Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymes
title_full_unstemmed Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymes
title_sort Glycosidase mechanisms: Sugar conformations and reactivity in endo- and exo-acting enzymes
dc.creator.none.fl_str_mv Abrahão Bueno Morais, Mariana
Nin Hill, Alba
Rovira i Virgili, Carme
author Abrahão Bueno Morais, Mariana
author_facet Abrahão Bueno Morais, Mariana
Nin Hill, Alba
Rovira i Virgili, Carme
author_role author
author2 Nin Hill, Alba
Rovira i Virgili, Carme
author2_role author
author
dc.subject.none.fl_str_mv Sucre
Dinàmica molecular
Enzims
Sugar
Molecular dynamics
Enzymes
topic Sucre
Dinàmica molecular
Enzims
Sugar
Molecular dynamics
Enzymes
description The enzymatic breakdown of carbohydrates plays a critical role in several biological events and enables the development of sustainable processes to obtain bioproducts and biofuels. In this scenario, the design of efficient inhibitors for glycosidases that can act as drug targets and the engineering of carbohydrate-active enzymes with tailored catalytic properties is of remarkable importance. To guide rational approaches, it is necessary to elucidate enzyme molecular mechanisms, in particular understanding how the microenvironment modulates the conformational space explored by the substrate. Computer simulations, especially those based on ab initio methods, have provided a suitable atomic description of carbohydrate conformations and catalytic reactions in several glycosidase families. In this review, we will focus on how the active-site topology (pocket or cleft) and mode of cleavage (endo or exo) can affect the catalytic mechanisms adopted by glycosidases, in particular the substrate conformations along the reaction coordinate.
publishDate 2023
dc.date.none.fl_str_mv 2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/219212
url https://hdl.handle.net/2445/219212
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.1016/j.cbpa.2023.102282
Current Opinion in Chemical Biology, 2023, vol. 74, p. 1-8
https://doi.org/10.1016/j.cbpa.2023.102282
dc.rights.none.fl_str_mv cc-by-nc-nd (c) Abrahão Bueno Morais, Mariana, et al., 2023
http://creativecommons.org/licenses/by-nc-nd/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by-nc-nd (c) Abrahão Bueno Morais, Mariana, et al., 2023
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv Articles publicats en revistes (Química Inorgànica i Orgànica)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.81155

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