Evidence map›Paper›PMID 24461779›Full record

ArticlePhytochemistry2014

High level protein-purification allows the unambiguous polypeptide determination of latent isoform PPO4 of mushroom tyrosinase.

Stephan G Mauracher, Christian Molitor, Claudia Michael, Martin Kragl, Andreas Rizzi, Annette Rompel

Open access · hybridAbstract read
In one paragraph

Article in Phytochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  8. Review
  9. Molecules (Basel, Switzerland) · 2020
    Article
  10. Article
  11. Article
  12. Lectins from the Edible MushroomMolecules (Basel, Switzerland) · 2020
    Review
  13. A Peptide-Induced Self-Cleavage Reaction Initiates the Activation of Tyrosinase.Angewandte Chemie (International ed. in English) · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
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  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Stephan G MauracherDepartment of Biophysical Chemistry, University of Vienna, Althanstraße 14, 1090 Vienna, Austria.
Christian MolitorDepartment of Biophysical Chemistry, University of Vienna, Althanstraße 14, 1090 Vienna, Austria.
Claudia MichaelDepartment of Analytical Chemistry, University of Vienna, Währinger Straße 38, 1090 Vienna, Austria.
Martin KraglDepartment of Biophysical Chemistry, University of Vienna, Althanstraße 14, 1090 Vienna, Austria.
Andreas RizziDepartment of Analytical Chemistry, University of Vienna, Währinger Straße 38, 1090 Vienna, Austria.
Annette RompelDepartment of Biophysical Chemistry, University of Vienna, Althanstraße 14, 1090 Vienna, Austria. Electronic address: annette.rompel@univie.ac.at.
University of Vienna · AT

Funding

Austrian Science Fund FWF P 25217
6 · The paper itself

Abstract

Tyrosinases catalyze two initial reaction steps in the formation of melanin. Purification of tyrosinases had always been a process accompanied with various problems caused by enzymatic browning processes. Here, an approach is presented for the purification of the latent enzyme from mushrooms which averts and removes interfering compounds (e.g. polyphenols) in advance to the extraction process. The described method is supposed being well suitable as a general protein purification protocol from natural sources like fungi and plants. The purified enzyme was investigated in detail by means of mass spectrometry: its intact protein mass was determined as 64,247.3 Da and it was identified as number four of in total six isoforms (PPO1-6) by means of sequence analysis. Some PTMs, strain specific sequence disparities and several cleavage sites including the one causing enzyme-activation (Ser³⁸³) were determined, thus, providing insights on the maturation process of this latent tyrosinase zymogen. Based on these sequence data it can be concluded that the polypeptide backbone of the latent form of the tyrosinase PPO4 ranges from Ser² to Thr⁵⁶⁵, missing when compared to the gene-derived sequence a small part (46 amino acids) of the C-terminal tail. The high content on hydrophobic amino acids within this missing tail gives rise to speculations whether this part might have a function as a membrane anchor.

Indexed as

AgaricalesBiocatalysisIsoenzymesModels, MolecularMonophenol MonooxygenasePeptidesIsoenzymesMonophenol MonooxygenasePeptidesAgaricus bisporusLatent tyrosinaseMetalloenzymePolyphenolsPost translational modificationPPO4Protease inhibitorType-3 copper centerTyrosinase maturationZymogen

Identifiers

PMID24461779
PMCPMC3969299
OpenAlexW2065232892

What OpenQuestion holds

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LicenceCC BY
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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.