Evidence map›Paper›PMID 27896501›Full record

ArticleExtremophiles : life under extreme conditions2017

A manganese catalase from Thermomicrobium roseum with peroxidase and catecholase activity.

Robin Baginski, Monika Sommerhalter

Abstract read
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In one paragraph

Article in Extremophiles : life under extreme conditions, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

4 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Theoretical study of the mechanism of the manganese catalase KatB.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Article
  4. 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

2 authors at 1 institution in 1 country.

Robin BaginskiDepartment of Chemistry and Biochemistry, California State University East Bay, Hayward, CA, 94542, USA.
Monika SommerhalterDepartment of Chemistry and Biochemistry, California State University East Bay, Hayward, CA, 94542, USA. monika.sommerhalter@csueastbay.edu.
California State University, East Bay · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An enzyme with catechol oxidase activity was identified in Thermomicrobium roseum extracts via solution assays and activity-stained SDS-PAGE. Yet, the genome of T. roseum does not harbor a catecholase gene. The enzyme was purified with two anion exchange chromatography steps and ultimately identified to be a manganese catalase with additional peroxidase and catecholase activity. Catalase activity (6280 ± 430 IU/mg) clearly dominated over pyrogallol peroxidase (231 ± 53 IU/mg) and catecholase (3.07 ± 0.56 IU/mg) activity as determined at 70 °C. Most enzyme kinetic properties were comparable to previously characterized manganese catalase enzymes. Catalase activity was highest at alkaline pH values and showed inhibition by excess substrate and chloride. The apparent K

Indexed as

Bacterial ProteinsCatalaseCatecholsChloroflexiEnzyme StabilityHot TemperatureHydrogen-Ion ConcentrationPeroxidasePyrogallolSubstrate SpecificityBacterial ProteinsCatalasecatecholCatecholsPeroxidasePyrogallolCatalase-phenol oxidaseCatecholaseManganese catalasePeroxidaseThermomicrobium roseum

Identifiers

PMID27896501
OpenAlexW2557512342

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.