Evidence map›Paper›PMID 32616720›Full record

ArticleScientific reports2020

Identification of the amino acid position controlling the different enzymatic activities in walnut tyrosinase isoenzymes (jrPPO1 and jrPPO2).

Felix Panis, Annette Rompel

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 29 citations in OpenAlex.

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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.

Felix PanisUniversität 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.
University of Vienna · AT

Funding

Austrian Science Fund FWF P 29144Austrian Science Fund FWF P29144
6 · The paper itself

Abstract

Polyphenol oxidases (PPOs) are ubiquitously distributed among plants, bacteria, fungi and animals. They catalyze the hydroxylation of monophenols (monophenolase activity) and the oxidation of o-diphenols (diphenolase activity) to o-quinones. PPOs are commonly present as an isoenzyme family. In walnut (Juglans regia), two different genes (jrPPO1 and jrPPO2) encoding PPOs have been identified. In this study, jrPPO2 was, for the first time, heterologously expressed in E. coli and characterized as a tyrosinase (TYR) by substrate scope assays and kinetic investigations, as it accepted tyramine and L-tyrosine as substrates. Moreover, the substrate acceptance and kinetic parameters (k

Indexed as

Monophenol MonooxygenaseAmino Acid SequenceCatalysisCatechol OxidaseEscherichia coliIsoenzymesJuglansMolecular Docking SimulationMutationPhenolsSubstrate SpecificityTyramineTyrosineCatechol OxidaseIsoenzymesMonophenol MonooxygenasePhenolsTyramineTyrosine

Identifiers

PMID32616720
PMCPMC7331820
OpenAlexW3039663336

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.