Evidence map›Paper›PMID 30056630›Full record

ArticleProtein science : a publication of the Protein Society2019

Tyrosine substitution of a conserved active-site histidine residue activates Plasmodium falciparum peroxiredoxin 6.

Kristina Feld, Fabian Geissel, Linda Liedgens, Robin Schumann, Sandra Specht, Marcel Deponte

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 52% 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

2 citing papers in PubMed, 12 citations in OpenAlex.

  1. HAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  2. 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

6 authors at 2 institutions in 1 country.

Kristina FeldDepartment of Parasitology, Ruprecht-Karls University, D-69120, Heidelberg, Germany.
Fabian GeisselFaculty of Chemistry/Biochemistry, TU Kaiserslautern, D-67663, Kaiserslautern, Germany.
Linda LiedgensDepartment of Parasitology, Ruprecht-Karls University, D-69120, Heidelberg, Germany.
Robin SchumannFaculty of Chemistry/Biochemistry, TU Kaiserslautern, D-67663, Kaiserslautern, Germany.
Sandra SpechtDepartment of Parasitology, Ruprecht-Karls University, D-69120, Heidelberg, Germany.
Marcel DeponteDepartment of Parasitology, Ruprecht-Karls University, D-69120, Heidelberg, Germany.
University of Kaiserslautern · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxiredoxins efficiently remove hydroperoxides and peroxynitrite in pro- and eukaryotes. However, isoforms of one subfamily of peroxiredoxins, the so-called Prx6-type enzymes, usually have very low activities in standard peroxidase assays in vitro. In contrast to other peroxiredoxins, Prx6 homologues share a conserved histidyl residue at the bottom of the active site. Here we addressed the role of this histidyl residue for redox catalysis using the Plasmodium falciparum homologue PfPrx6 as a model enzyme. Steady-state kinetics with tert-butyl hydroperoxide (tBuOOH) revealed that the histidyl residue is nonessential for Prx6 catalysis and that a replacement with tyrosine can even increase the enzyme activity four- to six-fold in vitro. Stopped-flow kinetics with reduced PfPrx6

Indexed as

Amino Acid SubstitutionCatalytic DomainEnzyme ActivationGain of Function MutationHistidineHydrogen PeroxideKineticsOxidation-ReductionPeroxiredoxin VIPlasmodium falciparumProtozoan ProteinsTyrosineHistidineHydrogen PeroxidePeroxiredoxin VIProtozoan ProteinsTyrosine1-Cys Prxenzyme mechanismperoxiredoxin catalysisPlasmodium falciparumPrx6steady-state kineticsstopped-flow kinetics

Identifiers

PMID30056630
PMCPMC6295898
OpenAlexW2884720805

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.