Evidence map›Paper›PMID 33188177›Full record

ArticleNature communications2020

Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs).

Riin Kont, Bastien Bissaro, Vincent G H Eijsink, Priit Väljamäe

Abstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
–field-weighted citation impact
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

45 citing papers in PubMed.

  1. Article
  2. Review
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  4. Article
  5. Redox robustness drives LPMO evolution.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  7. Article
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  16. Review
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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

4 authors.

Riin KontInstitute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.
Bastien BissaroFaculty of Chemistry, Biotechnology and Food Science, NMBU-Norwegian University of Life Sciences, Ås, Norway.ORCID 0000-0001-8354-3892
Vincent G H EijsinkFaculty of Chemistry, Biotechnology and Food Science, NMBU-Norwegian University of Life Sciences, Ås, Norway.ORCID 0000-0002-9220-8743
Priit VäljamäeInstitute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia. priit.valjamae@ut.ee.ORCID 0000-0002-1035-9493

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are widely distributed in Nature, where they catalyze the hydroxylation of glycosidic bonds in polysaccharides. Despite the importance of LPMOs in the global carbon cycle and in industrial biomass conversion, the catalytic properties of these monocopper enzymes remain enigmatic. Strikingly, there is a remarkable lack of kinetic data, likely due to a multitude of experimental challenges related to the insoluble nature of LPMO substrates, like cellulose and chitin, and to the occurrence of multiple side reactions. Here, we employed competition between well characterized reference enzymes and LPMOs for the H

Indexed as

BacteriaCatalaseCelluloseChitinFungiHorseradish PeroxidaseHydrogen PeroxideKineticsMixed Function OxygenasesNanoparticlesSubstrate SpecificityCatalaseCelluloseChitinHorseradish PeroxidaseHydrogen PeroxideMixed Function Oxygenasesperoxygenase

Identifiers

PMID33188177
PMCPMC7666214

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.