Applications and insights of NMR in enzyme engineering and biocatalysis

In order to be used in biocatalysis, natural or de novo enzymes must be engineered to function under the desired reaction conditions. Rational enzyme design draws on experimental data such as structure, mechanism and sequence to identify promising hotspots, thereby reducing the number of variants th...

Descripción completa

Detalles Bibliográficos
Autores: Pérez, Yolanda, Moreno, Carlos J., Clapés, Pere
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2026
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/424384
Acceso en línea:http://hdl.handle.net/10261/424384
https://api.elsevier.com/content/abstract/scopus_id/105032443716
Access Level:acceso abierto
Palabra clave:Rational design
Biocatalysis
NMR
Protein engineering
http://metadata.un.org/sdg/3
http://metadata.un.org/sdg/9
Ensure healthy lives and promote well-being for all at all ages
Build resilient infrastructure, promote inclusive and sustainable industrialization and foster innovation
id ES_795d647d05bf4fa540af4fcfdc18f68c
oai_identifier_str oai:digital.csic.es:10261/424384
network_acronym_str ES
network_name_str España
repository_id_str
spelling Applications and insights of NMR in enzyme engineering and biocatalysisPérez, YolandaMoreno, Carlos J.Clapés, PereRational designBiocatalysisNMRProtein engineeringhttp://metadata.un.org/sdg/3http://metadata.un.org/sdg/9Ensure healthy lives and promote well-being for all at all agesBuild resilient infrastructure, promote inclusive and sustainable industrialization and foster innovationIn order to be used in biocatalysis, natural or de novo enzymes must be engineered to function under the desired reaction conditions. Rational enzyme design draws on experimental data such as structure, mechanism and sequence to identify promising hotspots, thereby reducing the number of variants that need to be tested to improve the desired properties. Enzymes are dynamic and exist as ensembles of low-energy conformations in equilibrium with sparsely populated transient high-energy states that are often undetectable by experimental techniques targeting static native structures. Moreover, enzyme function is influenced not only by active-site residues but also by second, third, and outer-shell residues, which regulate structural dynamics and conformational sampling. Alternative conformations such as side-chain rotamers, loop rearrangements, and folding variations can enable functions like non-native ligand recognition. Historically, the incorporation of experimental structural dynamics information into enzyme engineering for abiotic catalysis was limited by the complexity and low throughput of nuclear magnetic resonance (NMR) structural analysis. This review highlights the diverse applications and emerging NMR approaches that enhance our understanding of enzyme conformational ensembles. It also covers the development of robust methodologies that allow the changes associated with the laboratory evolution of enzymes to be assessed more rapidly. These advances significantly increase NMR throughput, enabling broader applications in underutilized areas such as enzyme evolution and engineering.This work was supported by funding from the Grant PID2024-155168NB-I00 funded by MCIN/AEI/10.13039/501100011033, and by “ERDF A way of making Europe.”Peer reviewedTaylor & FrancisMinisterio de Ciencia e Innovación (España)0000-0003-3767-5346Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202620262026info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/424384https://api.elsevier.com/content/abstract/scopus_id/105032443716reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MCIN/AEI/10.13039Biocatalysis and Biotransformationhttps://doi.org/10.1080/10242422.2026.2639009Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/4243842026-05-22T06:33:51Z
dc.title.none.fl_str_mv Applications and insights of NMR in enzyme engineering and biocatalysis
title Applications and insights of NMR in enzyme engineering and biocatalysis
spellingShingle Applications and insights of NMR in enzyme engineering and biocatalysis
Pérez, Yolanda
Rational design
Biocatalysis
NMR
Protein engineering
http://metadata.un.org/sdg/3
http://metadata.un.org/sdg/9
Ensure healthy lives and promote well-being for all at all ages
Build resilient infrastructure, promote inclusive and sustainable industrialization and foster innovation
title_short Applications and insights of NMR in enzyme engineering and biocatalysis
title_full Applications and insights of NMR in enzyme engineering and biocatalysis
title_fullStr Applications and insights of NMR in enzyme engineering and biocatalysis
title_full_unstemmed Applications and insights of NMR in enzyme engineering and biocatalysis
title_sort Applications and insights of NMR in enzyme engineering and biocatalysis
dc.creator.none.fl_str_mv Pérez, Yolanda
Moreno, Carlos J.
Clapés, Pere
author Pérez, Yolanda
author_facet Pérez, Yolanda
Moreno, Carlos J.
Clapés, Pere
author_role author
author2 Moreno, Carlos J.
Clapés, Pere
author2_role author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia e Innovación (España)
0000-0003-3767-5346
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Rational design
Biocatalysis
NMR
Protein engineering
http://metadata.un.org/sdg/3
http://metadata.un.org/sdg/9
Ensure healthy lives and promote well-being for all at all ages
Build resilient infrastructure, promote inclusive and sustainable industrialization and foster innovation
topic Rational design
Biocatalysis
NMR
Protein engineering
http://metadata.un.org/sdg/3
http://metadata.un.org/sdg/9
Ensure healthy lives and promote well-being for all at all ages
Build resilient infrastructure, promote inclusive and sustainable industrialization and foster innovation
description In order to be used in biocatalysis, natural or de novo enzymes must be engineered to function under the desired reaction conditions. Rational enzyme design draws on experimental data such as structure, mechanism and sequence to identify promising hotspots, thereby reducing the number of variants that need to be tested to improve the desired properties. Enzymes are dynamic and exist as ensembles of low-energy conformations in equilibrium with sparsely populated transient high-energy states that are often undetectable by experimental techniques targeting static native structures. Moreover, enzyme function is influenced not only by active-site residues but also by second, third, and outer-shell residues, which regulate structural dynamics and conformational sampling. Alternative conformations such as side-chain rotamers, loop rearrangements, and folding variations can enable functions like non-native ligand recognition. Historically, the incorporation of experimental structural dynamics information into enzyme engineering for abiotic catalysis was limited by the complexity and low throughput of nuclear magnetic resonance (NMR) structural analysis. This review highlights the diverse applications and emerging NMR approaches that enhance our understanding of enzyme conformational ensembles. It also covers the development of robust methodologies that allow the changes associated with the laboratory evolution of enzymes to be assessed more rapidly. These advances significantly increase NMR throughput, enabling broader applications in underutilized areas such as enzyme evolution and engineering.
publishDate 2026
dc.date.none.fl_str_mv 2026
2026
2026
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/10261/424384
https://api.elsevier.com/content/abstract/scopus_id/105032443716
url http://hdl.handle.net/10261/424384
https://api.elsevier.com/content/abstract/scopus_id/105032443716
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MCIN/AEI/10.13039
Biocatalysis and Biotransformation
https://doi.org/10.1080/10242422.2026.2639009
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Taylor & Francis
publisher.none.fl_str_mv Taylor & Francis
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
_version_ 1869411343334899712
score 15,198674

Similares en LA Referencia