Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases

Glycoside hydrolases and glycosyltransferases are the main classes of enzymes that synthesize and degrade carbohydrates, molecules essential to life that are a challenge for classical chemistry. As such, considerable efforts have been made to engineer these enzymes and make them pliable to human nee...

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Detalles Bibliográficos
Autores: Coines, Joan, Cuxart Sanchez, Irene, Teze, David, Rovira i Virgili, Carme
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2022
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/214307
Acceso en línea:https://hdl.handle.net/2445/214307
Access Level:acceso abierto
Palabra clave:Fosfats
Pèptids
Proteïnes
Phosphates
Peptides
Proteins
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spelling Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and GlycosyltransferasesCoines, JoanCuxart Sanchez, IreneTeze, DavidRovira i Virgili, CarmeFosfatsPèptidsProteïnesPhosphatesPeptidesProteinsGlycoside hydrolases and glycosyltransferases are the main classes of enzymes that synthesize and degrade carbohydrates, molecules essential to life that are a challenge for classical chemistry. As such, considerable efforts have been made to engineer these enzymes and make them pliable to human needs, ranging from directed evolution to rational design, including mechanism engineering. Such endeavors fall short and are unreported in numerous cases, while even success is a necessary but not sufficient proof that the chemical rationale behind the design is correct. Here we review some of the recent work in CAZyme mechanism engineering, showing that computational simulations are instrumental to rationalize experimental data, providing mechanistic insight into how native and engineered CAZymes catalyze chemical reactions. We illustrate this with two recent studies in which (i) a glycoside hydrolase is converted into a glycoside phosphorylase and (ii) substrate specificity of a glycosyltransferase is engineered toward forming O-, N-, or S-glycosidic bonds.American Chemical Society2024202420222024info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersion11 p.application/pdfhttps://hdl.handle.net/2445/214307Articles publicats en revistes (Química Inorgànica i Orgànica)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésVersió postprint del document publicat a: https://doi.org/10.1021/acs.jpcb.1c09536Journal of Physical Chemistry B, 2022, vol. 126, num.4, p. 802-812https://doi.org/10.1021/acs.jpcb.1c09536(c) American Chemical Society, 2022info:eu-repo/semantics/openAccessoai:recercat.cat:2445/2143072026-05-29T05:05:01Z
dc.title.none.fl_str_mv Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases
title Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases
spellingShingle Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases
Coines, Joan
Fosfats
Pèptids
Proteïnes
Phosphates
Peptides
Proteins
title_short Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases
title_full Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases
title_fullStr Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases
title_full_unstemmed Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases
title_sort Computer Simulation to Rationalize "Rational" Engineering of Glycoside Hydrolases and Glycosyltransferases
dc.creator.none.fl_str_mv Coines, Joan
Cuxart Sanchez, Irene
Teze, David
Rovira i Virgili, Carme
author Coines, Joan
author_facet Coines, Joan
Cuxart Sanchez, Irene
Teze, David
Rovira i Virgili, Carme
author_role author
author2 Cuxart Sanchez, Irene
Teze, David
Rovira i Virgili, Carme
author2_role author
author
author
dc.subject.none.fl_str_mv Fosfats
Pèptids
Proteïnes
Phosphates
Peptides
Proteins
topic Fosfats
Pèptids
Proteïnes
Phosphates
Peptides
Proteins
description Glycoside hydrolases and glycosyltransferases are the main classes of enzymes that synthesize and degrade carbohydrates, molecules essential to life that are a challenge for classical chemistry. As such, considerable efforts have been made to engineer these enzymes and make them pliable to human needs, ranging from directed evolution to rational design, including mechanism engineering. Such endeavors fall short and are unreported in numerous cases, while even success is a necessary but not sufficient proof that the chemical rationale behind the design is correct. Here we review some of the recent work in CAZyme mechanism engineering, showing that computational simulations are instrumental to rationalize experimental data, providing mechanistic insight into how native and engineered CAZymes catalyze chemical reactions. We illustrate this with two recent studies in which (i) a glycoside hydrolase is converted into a glycoside phosphorylase and (ii) substrate specificity of a glycosyltransferase is engineered toward forming O-, N-, or S-glycosidic bonds.
publishDate 2022
dc.date.none.fl_str_mv 2022
2024
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/214307
url https://hdl.handle.net/2445/214307
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: https://doi.org/10.1021/acs.jpcb.1c09536
Journal of Physical Chemistry B, 2022, vol. 126, num.4, p. 802-812
https://doi.org/10.1021/acs.jpcb.1c09536
dc.rights.none.fl_str_mv (c) American Chemical Society, 2022
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) American Chemical Society, 2022
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 11 p.
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv Articles publicats en revistes (Química Inorgànica i Orgànica)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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