Evidence map›Paper›PMID 22330759›Full record

ReviewArchives of biochemistry and biophysics2012

Molecular evolution of hydrogen peroxide degrading enzymes.

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

Abstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed, 1 pooled it
–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

77 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Myeloperoxidase G463A polymorphism and lung cancer risk in Asians: a pooled analysis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013
    Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. The Structural Biology of Catalase Evolution.Sub-cellular biochemistry · 2024
    Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Physiological roles of catalases Cat1 and Cat2 in Myxococcus xanthus.Journal of microbiology (Seoul, Korea) · 2022
    Article

17 more citing papers are in PubMed but not listed here.

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.

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

Funding

Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

For efficient removal of intra- and/or extracellular hydrogen peroxide by dismutation to harmless dioxygen and water (2H(2)O(2) → O(2) + 2H(2)O), nature designed three metalloenzyme families that differ in oligomeric organization, monomer architecture as well as active site geometry and catalytic residues. Here we report on the updated reconstruction of the molecular phylogeny of these three gene families. Ubiquitous typical (monofunctional) heme catalases are found in all domains of life showing a high structural conservation. Their evolution was directed from large subunit towards small subunit proteins and further to fused proteins where the catalase fold was retained but lost its original functionality. Bifunctional catalase-peroxidases were at the origin of one of the two main heme peroxidase superfamilies (i.e. peroxidase-catalase superfamily) and constitute a protein family predominantly present among eubacteria and archaea, but two evolutionary branches are also found in the eukaryotic world. Non-heme manganese catalases are a relatively small protein family with very old roots only present among bacteria and archaea. Phylogenetic analyses of the three protein families reveal features typical (i) for the evolution of whole genomes as well as (ii) for specific evolutionary events including horizontal gene transfer, paralog formation and gene fusion. As catalases have reached a striking diversity among prokaryotic and eukaryotic pathogens, understanding their phylogenetic and molecular relationship and function will contribute to drug design for prevention of diseases of humans, animals and plants.

Indexed as

Bacterial ProteinsCatalaseCatalytic DomainEscherichia coli ProteinsEvolution, MolecularGene Transfer TechniquesHemeHydrogen PeroxideManganeseModels, ChemicalPeroxidasePhylogenyProteinsSequence Analysis, DNABacterial ProteinsCatalaseEscherichia coli ProteinsHemeHydrogen PeroxidekatG protein, E coliManganesePeroxidaseProteins

Identifiers

PMID22330759
PMCPMC3523812

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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.