Evidence map›Paper›PMID 28154175›Full record

ArticleThe Journal of biological chemistry2017

Pre-steady-state Kinetics Reveal the Substrate Specificity and Mechanism of Halide Oxidation of Truncated Human Peroxidasin 1.

Martina Paumann-Page, Romy-Sophie Katz, Marzia Bellei, Irene Schwartz, Eva Edenhofer, Benjamin Sevcnikar, Monika Soudi, Stefan Hofbauer, Gianantonio Battistuzzi, Paul G Furtmüller and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

16 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The role of peroxidasin in solid cancer progression.Biochemical Society transactions · 2023
    Review
  5. Article
  6. The oxidative stress response ofFrontiers in microbiology · 2023
    Review
  7. Article
  8. Article
  9. Review
  10. Inhibition of Myeloperoxidase.Handbook of experimental pharmacology · 2021
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Secreted heme peroxidase fromThe Journal of biological chemistry · 2018
    Article
  16. Review
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

11 authors at 2 institutions in 4 countries.

Martina Paumann-PageFrom the Department of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria and.
Romy-Sophie KatzFrom the Department of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria and.
Marzia Belleithe Departments of Life Sciences and.
Irene SchwartzFrom the Department of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria and.
Eva EdenhoferFrom the Department of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria and.
Benjamin SevcnikarFrom the Department of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria and.
Monika SoudiFrom the Department of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria and.
Stefan HofbauerFrom the Department of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria and.ORCID 0000-0003-3375-7715
Gianantonio BattistuzziChemistry and Geology, University of Modena and Reggio Emilia, 41125 Modena, Italy.ORCID 0000-0003-4716-5745
Paul G FurtmüllerFrom the Department of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria and paul.furtmueller@boku.ac.at.ORCID 0000-0002-1199-2469
Christian ObingerFrom the Department of Chemistry, Division of Biochemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria and christian.obinger@boku.ac.at.ORCID 0000-0002-7133-3430
BOKU University · ATUniversity of Modena and Reggio Emilia · IT

Funding

Austrian Science Fund FWF P 25538Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Human peroxidasin 1 is a homotrimeric multidomain peroxidase that is secreted to the extracellular matrix. The heme enzyme was shown to release hypobromous acid that mediates the formation of specific covalent sulfilimine bonds to reinforce collagen IV in basement membranes. Maturation by proteolytic cleavage is known to activate the enzyme. Here, we present the first multimixing stopped-flow study on a fully functional truncated variant of human peroxidasin 1 comprising four immunoglobulin-like domains and the catalytically active peroxidase domain. The kinetic data unravel the so far unknown substrate specificity and mechanism of halide oxidation of human peroxidasin 1. The heme enzyme is shown to follow the halogenation cycle that is induced by the rapid H

Indexed as

BromidesCatalytic DomainChloridesCollagen Type IVExtracellular Matrix ProteinsFerric CompoundsHalogenationHumansHydrogen PeroxideIodidesKineticsOxidation-ReductionPeroxidasePeroxidasinProtein DomainsSubstrate SpecificityBromidesChloridesCollagen Type IVExtracellular Matrix ProteinsFerric CompoundsHydrogen PeroxideIodidesPeroxidasePeroxidasinthiocyanateThiocyanatesenzyme catalysisextracellular matrixhemekineticsperoxidase

Identifiers

PMID28154175
PMCPMC5377774
OpenAlexW2583740773

What OpenQuestion 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 OpenQuestion graph.