Evidence map›Paper›PMID 28821733›Full record

ArticleScientific reports2017

Three recombinantly expressed apple tyrosinases suggest the amino acids responsible for mono- versus diphenolase activity in plant polyphenol oxidases.

Ioannis Kampatsikas, Aleksandar Bijelic, Matthias Pretzler, Annette Rompel

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Human recombinant tyrosinase destabilization caused by the double mutation R217Q/R402Q.Protein science : a publication of the Protein Society · 2025
    Article
  5. Fine mapping and identification of the geneFrontiers in plant science · 2025
    Article
  6. Article
  7. Extraction, Purification, and Characterization of Olive (Journal of agricultural and food chemistry · 2024
    Article
  8. Article
  9. Article
  10. Genome-Wide Analysis of the Polyphenol Oxidase Gene Family inAntioxidants (Basel, Switzerland) · 2023
    Article
  11. Article
  12. Olive Polyphenol Oxidase Gene Family.International journal of molecular sciences · 2023
    Article
  13. Article
  14. The Infestation of Olive Fruits byMolecules (Basel, Switzerland) · 2022
    Article
  15. Polyphenol oxidase and enzymatic browning in apricot (Current research in food science · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  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 1 country.

Ioannis KampatsikasUniversität Wien, Fakultät für Chemie, Institut für Biophysikalische Chemie, Althanstraße 14, 1090, Wien, Austria.
Aleksandar BijelicUniversität Wien, Fakultät für Chemie, Institut für Biophysikalische Chemie, Althanstraße 14, 1090, Wien, Austria.
Matthias PretzlerUniversität Wien, Fakultät für Chemie, Institut für Biophysikalische Chemie, Althanstraße 14, 1090, Wien, Austria.
Annette RompelUniversität Wien, Fakultät für Chemie, Institut für Biophysikalische Chemie, Althanstraße 14, 1090, Wien, Austria. annette.rompel@univie.ac.at.ORCID 0000-0002-5919-0553
University of Vienna · AT

Funding

Austrian Science Fund FWF P 25217Austrian Science Fund FWF P 29144
6 · The paper itself

Abstract

Tyrosinases and catechol oxidases belong to the polyphenol oxidase (PPO) enzyme family, which is mainly responsible for the browning of fruits. Three cDNAs encoding PPO pro-enzymes have been cloned from leaves of Malus domestica (apple, MdPPO). The three pro-enzymes MdPPO1-3 were heterologously expressed in E. coli yielding substantial amounts of protein and have been characterized with regard to their optimum of activity resulting from SDS, acidic and proteolytic activation. Significant differences were found in the kinetic characterization of MdPPO1-3 when applying different mono- and diphenolic substrates. All three enzymes have been classified as tyrosinases, where MdPPO1 exhibits the highest activity with tyramine (k

Indexed as

Recombinant ProteinsAmino AcidsAmino Acid SequenceCatechol OxidaseGene ExpressionMalusModels, MolecularMonophenol MonooxygenaseProtein ConformationProtoporphyrinogen OxidaseSpectrometry, Mass, Electrospray IonizationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSubstrate SpecificityAmino AcidsCatechol OxidaseMonophenol MonooxygenaseProtoporphyrinogen OxidaseRecombinant Proteins

Identifiers

PMID28821733
PMCPMC5562730
OpenAlexW2749519083

What OpenQuestion holds

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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.