English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/146903
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

DC FieldValueLanguage
dc.contributor.authorAyuso-Fernández, Iván-
dc.contributor.authorMartínez, Ángel T.-
dc.contributor.authorRuiz-Dueñas, F. J.-
dc.date.accessioned2017-03-16T17:03:05Z-
dc.date.available2017-03-16T17:03:05Z-
dc.date.issued2017-03-16-
dc.identifier.citationBiotechnology for Biofuels 10: 67 (2017)-
dc.identifier.issn1754-6834-
dc.identifier.urihttp://hdl.handle.net/10261/146903-
dc.description.abstract[Background] Floudas et al. (Science 336: 1715) established that lignin-degrading fungi appeared at the end of Carboniferous period associated with the production of the first ligninolytic peroxidases. Here, the subsequent evolution of these enzymes in Polyporales, where most wood-rotting fungi are included, is experimentally recreated using genomic information.-
dc.description.abstract[Results] With this purpose, we analyzed the evolutionary pathway leading to the most efficient lignin-degrading peroxidases characterizing Polyporales species. After sequence reconstruction from 113 genes of ten sequenced genomes, the main enzyme intermediates were resurrected and characterized. Biochemical changes were analyzed together with predicted sequences and structures, to understand how these enzymes acquired the ability to degrade lignin and how this ability changed with time. The most probable first peroxidase in Polyporales would be a manganese peroxidase (Mn3+ oxidizing phenolic lignin) that did not change substantially until the appearance of an exposed tryptophan (oxidizing nonphenolic lignin) originating an ancestral versatile peroxidase. Later, a quick evolution, with loss of the Mn2+-binding site, generated the first lignin peroxidase that evolved to the extant form by improving the catalytic efficiency. Increased stability at acidic pH, which strongly increases the oxidizing power of these enzymes, was observed paralleling the appearance of the exposed catalytic tryptophan.-
dc.description.abstract[Conclusions] We show how the change in peroxidase catalytic activities meant an evolutionary exploration for more efficient ways of lignin degradation by fungi, a key step for carbon recycling in land ecosystems. The study provides ancestral enzymes with a potential biotechnological interest for the sustainable production of fuels and chemicals in a biomass-based economy.-
dc.description.sponsorshipWe acknowledge support of the publication fee by the CSIC Open Access Publication Support Initiative through its Unit of Information Resources for Research (URICI), and the EC OpenAIRE FP7 post-grant Open Access Pilot.-
dc.description.sponsorshipThis work was supported by the INDOX (KBBE-2013-613549) and EnzOx2 (H2020-BBI-PPP-2015-2-720297) EU projects and the NOESIS (BIO2014-56388-R) project of the Spanish Ministry of Economy and Competitiveness (MINECO). The work conducted by JGI was supported by the Office of Science of the U.S. Department of Energy under Contract DE-AC02-05CH11231.-
dc.description.sponsorshipEUR 1,620 APC fee funded by the EC FP7 Post-Grant Open Access Pilot-
dc.publisherBioMed Central-
dc.relationFP7 post-grant Gold Open Access Pilot-
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/613549-
dc.relationinfo:eu-repo/grantAgreement/EC/H2020/720297-
dc.relationMINECO/ICTI2013-2016/BIO2014-56388-R-
dc.relation.isversionofPublisher's version-
dc.subjectLignin biodegradation resurrected enzymes-
dc.subjectCatalytic properties-
dc.subjectpH stability-
dc.subjectLigninolytic peroxidases-
dc.subjectAncestral sequence reconstruction-
dc.subjectFungal evolution-
dc.subjectFungal genomes-
dc.titleExperimental recreation of the evolution of lignin-degrading enzymes from the Jurassic to date-
dc.typeartículo-
dc.identifier.doi10.1186/s13068-017-0744-x-
dc.relation.publisherversionhttp://dx.doi.org/10.1186/s13068-017-0744-x-
dc.date.updated2017-03-16T17:03:06Z-
dc.language.rfc3066en-
dc.rights.holderThe Author(s)-
dc.rights.licensehttp://creativecommons.org/licenses/by/4.0/-
dc.contributor.funderEuropean Commission-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.contributor.funderDepartment of Energy (US)-
dc.relation.csic-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/100000015es_ES
Appears in Collections:(CIB) Artículos
Files in This Item:
File Description SizeFormat 
13068_2017_Article_744.pdf2,68 MBAdobe PDFThumbnail
View/Open
Show simple item record
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.