000064502 001__ 64502
000064502 005__ 20210121114542.0
000064502 0247_ $$2doi$$a10.3852/15-027
000064502 0248_ $$2sideral$$a103933
000064502 037__ $$aART-2015-103933
000064502 041__ $$aeng
000064502 100__ $$0(orcid)0000-0003-4076-6118$$aFerreira, Patricia$$uUniversidad de Zaragoza
000064502 245__ $$aA survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes
000064502 260__ $$c2015
000064502 5060_ $$aAccess copy available to the general public$$fUnrestricted
000064502 5203_ $$aThe genomes of three representative Polyporales (Bjerkandera adusta, Phlebia brevispora and a member of the Ganoderma lucidum complex) recently were sequenced to expand our knowledge on the diversity and distribution of genes involved in degradation of plant polymers in this Basidiomycota order, which includes most wood-rotting fungi. Oxidases, including members of the glucose-methanol-choline (GMC) oxidoreductase superfamily, play a central role in the above degradative process because they generate extracellular H2O2 acting as the ultimate oxidizer in both white-rot and brown-rot decay. The survey was completed by analyzing the GMC genes in the available genomes of seven more species to cover the four Polyporales clades. First, an in silico search for sequences encoding members of the aryl-alcohol oxidase, glucose oxidase, methanol oxidase, pyranose oxidase, cellobiose dehydrogenase and pyranose dehydrogenase families was performed. The curated sequences were subjected to an analysis of their evolutionary relationships, followed by estimation of gene duplication/ reduction history during fungal evolution. Second, the molecular structures of the near one hundred GMC oxidoreductases identified were modeled to gain insight into their structural variation and expected catalytic properties. In contrast to ligninolytic peroxidases, whose genes are present in all white-rot Polyporales genomes and absent from those of brown-rot species, the H2O2-generating oxidases are widely distributed in both fungal types. This indicates that the GMC oxidases provide H2O2 for both ligninolytic peroxidase activity (in white-rot decay) and Fenton attack on cellulose (in brown-rot decay), after the transition between both decay patterns in Polyporales occurred.
000064502 536__ $$9info:eu-repo/grantAgreement/ES/MICINN/BIO2011-26694$$9info:eu-repo/grantAgreement/EC/FP7/613549/EU/Optimized oxidoreductases for medium and large scale industrial biotransformations/INDOX
000064502 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
000064502 590__ $$a2.638$$b2015
000064502 591__ $$aMYCOLOGY$$b9 / 29 = 0.31$$c2015$$dQ2$$eT1
000064502 592__ $$a1.133$$b2015
000064502 593__ $$aMedicine (miscellaneous)$$c2015$$dQ1
000064502 593__ $$aPlant Science$$c2015$$dQ1
000064502 593__ $$aEcology, Evolution, Behavior and Systematics$$c2015$$dQ1
000064502 593__ $$aPhysiology$$c2015$$dQ2
000064502 593__ $$aGenetics$$c2015$$dQ2
000064502 593__ $$aMolecular Biology$$c2015$$dQ2
000064502 593__ $$aCell Biology$$c2015$$dQ3
000064502 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000064502 700__ $$aCarro, J.
000064502 700__ $$aSerrano, A.
000064502 700__ $$aMartinez, A.T.
000064502 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000064502 773__ $$g107, 6 (2015), 1105-1119$$pMycologia$$tMYCOLOGIA$$x0027-5514
000064502 8564_ $$s3515038$$uhttps://zaguan.unizar.es/record/64502/files/texto_completo.pdf$$yVersión publicada
000064502 8564_ $$s123040$$uhttps://zaguan.unizar.es/record/64502/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000064502 909CO $$ooai:zaguan.unizar.es:64502$$particulos$$pdriver
000064502 951__ $$a2021-01-21-11:16:47
000064502 980__ $$aARTICLE