Evidence map›Paper›PMID 24846396›Full record

ArticleCellular and molecular life sciences : CMLS2014

Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases.

Marcel Zámocký, Bernhard Gasselhuber, Paul G Furtmüller, Christian Obinger

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
10.3field-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

26 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Localization of heme biosynthesis in the diatomFrontiers in plant science · 2025
    Article
  3. Review
  4. Article
  5. Facile Synthesis of MagneticPharmaceutics · 2023
    Article
  6. Lignin-Modifying Enzymes inJournal of fungi (Basel, Switzerland) · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Characterization of a Dye-Decolorizing Peroxidase fromJournal of fungi (Basel, Switzerland) · 2021
    Article
  11. Article
  12. Phylogenomics of Plant-AssociatedFrontiers in microbiology · 2021
    Article
  13. Hybrid Heme Peroxidases from Rice Blast FungusAntioxidants (Basel, Switzerland) · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
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 at 1 institution in 2 countries.

Marcel ZámockýDivision of Biochemistry, Department of Chemistry, VIBT, Vienna Institute of BioTechnology, BOKU, University of Natural Resources and Life Sciences, Muthgasse 18, 1190, Vienna, Austria, marcel.zamocky@boku.ac.at.
Bernhard Gasselhuber
Paul G Furtmüller
Christian Obinger
BOKU University · AT

Funding

Austrian Science Fund FWF P 23855Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Heme peroxidases and catalases are key enzymes of hydrogen peroxide metabolism and signaling. Here, the reconstruction of the molecular evolution of the peroxidase-catalase superfamily (annotated in pfam as PF00141) based on experimentally verified as well as numerous newly available genomic sequences is presented. The robust phylogenetic tree of this large enzyme superfamily was obtained from 490 full-length protein sequences. Besides already well-known families of heme b peroxidases arranged in three main structural classes, completely new (hybrid type) peroxidase families are described being located at the border of these classes as well as forming (so far missing) links between them. Hybrid-type A peroxidases represent a minor eukaryotic subfamily from Excavates, Stramenopiles and Rhizaria sharing enzymatic and structural features of ascorbate and cytochrome c peroxidases. Hybrid-type B peroxidases are shown to be spread exclusively among various fungi and evolved in parallel with peroxidases in land plants. In some ascomycetous hybrid-type B peroxidases, the peroxidase domain is fused to a carbohydrate binding (WSC) domain. Both here described hybrid-type peroxidase families represent important turning points in the complex evolution of the whole peroxidase-catalase superfamily. We present and discuss their phylogeny, sequence signatures and putative biological function.

Indexed as

PhylogenyAmino Acid SequenceAnimalsCatalaseEvolution, MolecularHumansModels, MolecularMolecular Sequence DataPeroxidaseProtein ConformationSequence AlignmentCatalasePeroxidase

Identifiers

PMID24846396
PMCPMC4232752
OpenAlexW2032202498

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.