Trapping and retaining intermediates in glycosyltransferases

Glycosyltransferases (GTs) attach sugar molecules to a broad range of acceptors, generating a remarkable amount of structural diversity in biological systems. GTs are classified as either “retaining” or “inverting” enzymes. Most retaining GTs typically use an SNi mechanism. In a recent article in th...

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Detalles Bibliográficos
Autor: Guerin, Marcelo E.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/341637
Acceso en línea:http://hdl.handle.net/10261/341637
Access Level:acceso abierto
Palabra clave:Escherichia coli
Cell surface
Capsular polysaccharide
Glycolipid biosynthesis
Glycosyltransferase
CAZyme
Enzyme structure
Enzyme mechanism
Enzyme catalysis
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spelling Trapping and retaining intermediates in glycosyltransferasesGuerin, Marcelo E.Escherichia coliCell surfaceCapsular polysaccharideGlycolipid biosynthesisGlycosyltransferaseCAZymeEnzyme structureEnzyme mechanismEnzyme catalysisGlycosyltransferases (GTs) attach sugar molecules to a broad range of acceptors, generating a remarkable amount of structural diversity in biological systems. GTs are classified as either “retaining” or “inverting” enzymes. Most retaining GTs typically use an SNi mechanism. In a recent article in the JBC, Doyle et al. demonstrate a covalent intermediate in the dual-module KpsC GT (GT107) supporting a double displacement mechanism.Peer reviewedElsevierAmerican Society for Biochemistry and Molecular BiologyConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2024202420232024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/341637reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1016/j.jbc.2023.105006Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3416372026-05-22T06:33:51Z
dc.title.none.fl_str_mv Trapping and retaining intermediates in glycosyltransferases
title Trapping and retaining intermediates in glycosyltransferases
spellingShingle Trapping and retaining intermediates in glycosyltransferases
Guerin, Marcelo E.
Escherichia coli
Cell surface
Capsular polysaccharide
Glycolipid biosynthesis
Glycosyltransferase
CAZyme
Enzyme structure
Enzyme mechanism
Enzyme catalysis
title_short Trapping and retaining intermediates in glycosyltransferases
title_full Trapping and retaining intermediates in glycosyltransferases
title_fullStr Trapping and retaining intermediates in glycosyltransferases
title_full_unstemmed Trapping and retaining intermediates in glycosyltransferases
title_sort Trapping and retaining intermediates in glycosyltransferases
dc.creator.none.fl_str_mv Guerin, Marcelo E.
author Guerin, Marcelo E.
author_facet Guerin, Marcelo E.
author_role author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Escherichia coli
Cell surface
Capsular polysaccharide
Glycolipid biosynthesis
Glycosyltransferase
CAZyme
Enzyme structure
Enzyme mechanism
Enzyme catalysis
topic Escherichia coli
Cell surface
Capsular polysaccharide
Glycolipid biosynthesis
Glycosyltransferase
CAZyme
Enzyme structure
Enzyme mechanism
Enzyme catalysis
description Glycosyltransferases (GTs) attach sugar molecules to a broad range of acceptors, generating a remarkable amount of structural diversity in biological systems. GTs are classified as either “retaining” or “inverting” enzymes. Most retaining GTs typically use an SNi mechanism. In a recent article in the JBC, Doyle et al. demonstrate a covalent intermediate in the dual-module KpsC GT (GT107) supporting a double displacement mechanism.
publishDate 2023
dc.date.none.fl_str_mv 2023
2024
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/341637
url http://hdl.handle.net/10261/341637
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1016/j.jbc.2023.105006
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv Elsevier
American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,812429

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