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Insights on Laccase Engineering from Molecular Simulations: Towards a Binding Focused Strategy
dc.contributor.author | Monza, Emanuele |
dc.contributor.author | Lucas, Fatima |
dc.contributor.author | Camarero, Susana |
dc.contributor.author | Alejaldre, Lorea C. |
dc.contributor.author | Martínez, Angel T. |
dc.contributor.author | Guallar, Víctor |
dc.contributor.other | Barcelona Supercomputing Center |
dc.date.accessioned | 2016-03-14T17:07:38Z |
dc.date.available | 2016-03-30T00:30:55Z |
dc.date.issued | 2015-03-30 |
dc.identifier.issn | 1948-7185 |
dc.identifier.uri | http://hdl.handle.net/2117/84343 |
dc.description.abstract | Understanding the molecular determinants of enzyme performance is of primary importance for the rational design of ad hoc mutants. A novel approach, which combines efficient conformational sampling and quick reactivity scoring, is used here to shed light on how substrate oxidation was improved during the directed evolution experiment of a fungal laccase (from Pycnoporus cinnabarinus), an industrially relevant class of oxidoreductases. It is found that the enhanced activity of the evolved enzyme is mainly the result of substrate arrangement in the active site, with no important change in the redox potential of the T1 copper. Mutations at the active site shift the binding mode into a more buried substrate position and provide a more favorable electrostatic environment for substrate oxidation. As a consequence, engineering the binding event seems to be a viable way to in silico evolution of oxidoreductases. |
dc.description.sponsorship | This work has been funded by the EU projects INDOX (KBBE20137613549) and ERC 2009Adg25027PELE (to V.G) and the Spanish Ministry of Education and Science project CTQ201348287 (to V.G). |
dc.format.extent | 7 p. |
dc.language.iso | eng |
dc.publisher | ACS Publications |
dc.subject | Àrees temàtiques de la UPC::Enginyeria mecànica::Impacte ambiental |
dc.subject.lcsh | Oxidation--Methodology |
dc.subject.lcsh | Molecular dynamics |
dc.subject.other | In silico enzyme engineering |
dc.subject.other | Copper oxidoreductases |
dc.subject.other | PELE |
dc.subject.other | Substrate binding |
dc.subject.other | Substrate oxidation |
dc.subject.other | Directed evolution |
dc.title | Insights on Laccase Engineering from Molecular Simulations: Towards a Binding Focused Strategy |
dc.type | Article |
dc.subject.lemac | Dinàmica molecular |
dc.identifier.doi | 10.1021/acs.jpclett.5b00225 |
dc.description.peerreviewed | Peer Reviewed |
dc.relation.publisherversion | http://pubs.acs.org/doi/abs/10.1021/acs.jpclett.5b00225 |
dc.rights.access | Open Access |
dc.description.version | Postprint (author's final draft) |
dc.relation.projectid | info:eu-repo/grantAgreement/EC/FP7/613549/EU/Optimized oxidoreductases for medium and large scale industrial biotransformations/INDOX |
dc.relation.projectid | info:eu-repo/grantAgreement/EC/FP7/250277/EU/P.E.L.E (Protein Energy Landscape Exploration): a la carte drug design tools/PELE |
dc.relation.projectid | info:eu-repo/grantAgreement/MINECO//CTQ2013-48287-R/ES/DISENYO COMPUTACIONAL RACIONAL DE OXIDOREDUCTASAS PARA APLICACIONES INDUSTRIALES Y TECNOLOGICAS/ |
local.citation.publicationName | Journal of Physical Chemistry Letters |
local.citation.volume | 6 |
local.citation.number | 8 |
local.citation.startingPage | 1447 |
local.citation.endingPage | 1453 |
local.personalitzacitacio | true |
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