Show simple item record

dc.contributor.authorLucas, M. Fatima
dc.contributor.authorMonza, Emanuele
dc.contributor.authorJorgensen, Lise J.
dc.contributor.authorErnst, Heidi A.
dc.contributor.authorPiontek, Klaus
dc.contributor.authorBjerrum, Morten J.
dc.contributor.authorMartinez, Angel T.
dc.contributor.authorCamarero, Susana
dc.contributor.authorGuallar, Victor
dc.contributor.otherBarcelona Supercomputing Center
dc.date.accessioned2017-05-19T09:56:06Z
dc.date.available2018-02-10T01:30:41Z
dc.date.issued2017-02-10
dc.identifier.citationLucas, M. F. [et al.]. Simulating Substrate Recognition and Oxidation in Laccases: From Description to Design. "Journal of Chemical Theory and Computation", 10 Febrer 2017, vol. 13, núm. 3, p. 1462-1467.
dc.identifier.issn1549-9618
dc.identifier.urihttp://hdl.handle.net/2117/104639
dc.description.abstractTo meet the very specific requirements demanded by industry, proteins must be appropriately tailored. Engineering laccases, to improve the oxidation of small molecules, with applications in multiple fields, is, however, a difficult task. Most efforts have concentrated on increasing the redox potential of the enzyme, but in recent work, we have pursued an alternate strategy to engineering these biocatalysts. In particular, we have found that redesigning substrate binding at the T1 pocket, guided by in silico methodologies, to be a more consistent option. In this work, we evaluate the robustness of our computational approach to estimate activity, emphasizing the importance of the binding event in laccase reactivity. Strengths and weaknesses of the protocol are discussed along with its potential for scoring large numbers of protein sequences and thus its significance in protein engineering.
dc.description.sponsorshipThis study was supported by the OxiDesign (CTQ2013-48287-R) and NOESIS (BIO2014-56388-R) Spanish projects and the INDOX (KBBE-2013-7−613549) EU-project.
dc.format.extent6 p.
dc.language.isoeng
dc.subjectÀrees temàtiques de la UPC::Enginyeria biomèdica
dc.subject.lcshEnzyme complexes
dc.subject.lcshProteins--Analysis
dc.subject.otherProteins
dc.subject.otherOxidation
dc.subject.otherEnzyme
dc.titleSimulating Substrate Recognition and Oxidation in Laccases: From Description to Design
dc.typeArticle
dc.subject.lemacProteïnes--Investigació
dc.subject.lemacEnzims
dc.identifier.doi10.1021/acs.jctc.6b01158
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://pubs.acs.org/doi/ipdf/10.1021/acs.jctc.6b01158
dc.rights.accessOpen Access
dc.description.versionPostprint (author's final draft)
dc.relation.projectidinfo:eu-repo/grantAgreement/MINECO/1PE/CTQ2013-48287-R
dc.relation.projectidinfo:eu-repo/grantAgreement/MINECO/1PE/BIO2014-56388-R
upcommons.citation.publishedtrue
upcommons.citation.publicationNameJournal of Chemical Theory and Computation
upcommons.citation.volume13
upcommons.citation.number3
upcommons.citation.startingPage1462
upcommons.citation.endingPage1467


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record

All rights reserved. This work is protected by the corresponding intellectual and industrial property rights. Without prejudice to any existing legal exemptions, reproduction, distribution, public communication or transformation of this work are prohibited without permission of the copyright holder