Evidence map›Paper›PMID 22437835›Full record

ArticleThe Journal of biological chemistry2012

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

Elena Fernández-Fueyo, Francisco J Ruiz-Dueñas, Yuta Miki, María Jesús Martínez, Kenneth E Hammel, Angel T Martínez

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
10.5field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
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  3. The white rot basidiomyceteApplied and environmental microbiology · 2024
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  11. A Multiomic Approach to Understand HowJournal of fungi (Basel, Switzerland) · 2021
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  12. Article
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  14. Intracellular pathways for lignin catabolism in white-rot fungi.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Article
  16. Conserved white-rot enzymatic mechanism for wood decay in the Basidiomycota genus Pycnoporus.DNA research : an international journal for rapid publication of reports on genes and genomes · 2020
    Article
  17. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Elena Fernández-FueyoCentro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Ramiro de Maeztu 9, E-28040 Madrid, Spain.
Francisco J Ruiz-Dueñas
Yuta Miki
María Jesús Martínez
Kenneth E Hammel
Angel T Martínez
Consejo Superior de Investigaciones Científicas · ESCentro de Investigaciones Biológicas Margarita Salas · ESUnited States Department of Agriculture · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 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.

Indexed as

CatalysisCoriolaceaeEscherichia coliGenome, FungalLigninMultigene FamilyPeroxidaseRecombinant ProteinsLigninPeroxidaseRecombinant Proteins

Identifiers

PMID22437835
PMCPMC3351359
OpenAlexW2138728991

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.