Evidence map›Paper›PMID 31091286›Full record

ArticlePloS one2019

A family AA5_2 carbohydrate oxidase from Penicillium rubens displays functional overlap across the AA5 family.

Filip Mollerup, Ville Aumala, Kirsti Parikka, Yann Mathieu, Harry Brumer, Maija Tenkanen, Emma Master

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.9field-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

7 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. A Putative Lignin Copper Oxidase fromJournal of fungi (Basel, Switzerland) · 2021
    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

7 authors at 4 institutions in 2 countries.

Filip MollerupDepartment of Bioproducts and Biosystems, Aalto University, Aalto, Finland.ORCID 0000-0003-2035-7122
Ville AumalaDepartment of Bioproducts and Biosystems, Aalto University, Aalto, Finland.ORCID 0000-0001-7222-0107
Kirsti ParikkaDepartment of Food and Environmental Sciences, University of Helsinki, Helsinki, Finland.
Yann MathieuMichael Smith Laboratories, University of British Columbia, Vancouver, British Columbia, Canada.
Harry BrumerMichael Smith Laboratories, University of British Columbia, Vancouver, British Columbia, Canada.ORCID 0000-0002-0101-862X
Maija TenkanenDepartment of Food and Environmental Sciences, University of Helsinki, Helsinki, Finland.ORCID 0000-0003-2883-2717
Emma MasterDepartment of Bioproducts and Biosystems, Aalto University, Aalto, Finland.
Aalto University · FIUniversity of British Columbia · CAUniversity of Helsinki · FIUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Copper radical alcohol oxidases belonging to auxiliary activity family 5, subfamily 2 (AA5_2) catalyze the oxidation of galactose and galactosides, as well as aliphatic alcohols. Despite their broad applied potential, so far very few AA5_2 members have been biochemically characterized. We report the recombinant production and biochemical characterization of an AA5_2 oxidase from Penicillium rubens Wisconsin 54-1255 (PruAA5_2A), which groups within an unmapped clade phylogenetically distant from those comprising AA5_2 members characterized to date. PruAA5_2 preferentially oxidized raffinose over galactose; however, its catalytic efficiency was 6.5 times higher on glycolaldehyde dimer compared to raffinose. Deep sequence analysis of characterized AA5_2 members highlighted amino acid pairs correlated to substrate range and conserved within the family. Moreover, PruAA5_2 activity spans substrate preferences previously reported for AA5 subfamily 1 and 2 members, identifying possible functional overlap across the AA5 family.

Indexed as

Cloning, MolecularFungal ProteinsGalactoseGalactosidesHigh-Throughput Nucleotide SequencingOxidation-ReductionOxidoreductasesPenicilliumPhylogenyProtein EngineeringRaffinoseRecombinant ProteinsSequence Analysis, ProteinFungal ProteinsGalactoseGalactosidesOxidoreductasesRaffinoseRecombinant Proteins

Identifiers

PMID31091286
PMCPMC6519835
OpenAlexW2945597347

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.