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Title

Lignin-degrading peroxidases from the genome of the selective ligninolytic fungus Ceriporiopsis subvermispora

AuthorsFernández-Fueyo, Elena ; Ruiz-Dueñas, F. J. ; Miki, Yuta ; Martínez, María Jesús ; Hammel, Kenneth E.; Martínez, Ángel T.
KeywordsEnzyme catalysis
Enzyme structure
Fungi
Lignin degradation
Molecular
Modeling peroxidase
Delignification genome
Annotation
Genome Screening
ligninolysis
Issue Date11-May-2012
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry 287: 16903-16916(2012)
AbstractThe white-rot fungus Ceriporiopsis subvermispora delignifies lignocellulose with high selectivity, but until now it has appeared to lack the specialized peroxidases, termed lignin peroxidases (LiPs) and versatile peroxidases (VPs), that are generally thought important for ligninolysis. We screened the recently sequenced C. subvermispora genome for genes that encode peroxidases with a potential ligninolytic role. A total of 26 peroxidase genes was apparent after a structural-functional classification based on homology modeling and a search for diagnostic catalytic amino acid residues. In addition to revealing the presence of nine heme-thiolate peroxidase superfamily members and the unexpected absence of the dye-decolorizing peroxidase superfamily, the search showed that the C. subvermispora genome encodes 16 class II enzymes in the plant-fungal-bacterial peroxidase superfamily, where LiPs and VPs are classified. The 16 encoded enzymes include 13 putative manganese peroxidases and one generic peroxidase but most notably two peroxidases containing the catalytic tryptophan characteristic of LiPs and VPs. We expressed these two enzymes in Escherichia coli and determined their substrate specificities on typical LiP/VP substrates, including nonphenolic lignin model monomers and dimers, as well as synthetic lignin. The results show that the two newly discovered C. subvermispora peroxidases are functionally competent LiPs and also suggest that they are phylogenetically and catalytically intermediate between classical LiPs and VPs. These results offer new insight into selective lignin degradation by C. subvermispora.
Description16 p.-8 fig.-1 tab.
Publisher version (URL)http://dx.doi.org/ 10.1074/jbc.M112.356378
URIhttp://hdl.handle.net/10261/50027
DOI10.1074/jbc.M112.356378
ISSN0021-9258
E-ISSN1083-351X
Appears in Collections:(CIB) Artículos
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