Evidence map›Paper›PMID 26680532›Full record

ArticleNature communications2015

Structure-function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family.

DeLu Tyler Yin, Saioa Urresti, Mickael Lafond, Esther M Johnston, Fatemeh Derikvand, Luisa Ciano, Jean-Guy Berrin, Bernard Henrissat, Paul H Walton, Gideon J Davies and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
12.4field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 103 citations in OpenAlex.

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  16. Tunable Production of (ACS catalysis · 2022
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  20. A LignocellulolyticJournal 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

11 authors at 5 institutions in 4 countries.

DeLu Tyler YinMichael Smith Laboratories and Department of Chemistry, University of British Columbia, 2185 East Mall, Vancouver, British Columbia, Canada V6T 1Z4.
Saioa UrrestiDepartment of Chemistry, University of York, Heslington, York YO10 5DD, UK.
Mickael LafondMichael Smith Laboratories and Department of Chemistry, University of British Columbia, 2185 East Mall, Vancouver, British Columbia, Canada V6T 1Z4.
Esther M JohnstonDepartment of Chemistry, University of York, Heslington, York YO10 5DD, UK.
Fatemeh DerikvandMichael Smith Laboratories and Department of Chemistry, University of British Columbia, 2185 East Mall, Vancouver, British Columbia, Canada V6T 1Z4.
Luisa CianoDepartment of Chemistry, University of York, Heslington, York YO10 5DD, UK.
Jean-Guy BerrinINRA, UMR1163 Biodiversité et Biotechnologie Fongiques Marseille F-13288, France.
Bernard HenrissatArchitecture et Fonction des Macromolécules Biologiques, CNRS-Aix-Marseille University, 163 Avenue de Luminy, Marseille 13288, France.
Paul H WaltonDepartment of Chemistry, University of York, Heslington, York YO10 5DD, UK.
Gideon J DaviesDepartment of Chemistry, University of York, Heslington, York YO10 5DD, UK.
Harry BrumerMichael Smith Laboratories and Department of Chemistry, University of British Columbia, 2185 East Mall, Vancouver, British Columbia, Canada V6T 1Z4.
University of York · GBUniversity of British Columbia · CABiodiversité et Biotechnologie Fongiques · FRCanada's Michael Smith Genome Sciences Centre · CACentre National de la Recherche Scientifique · FR

Funding

Biotechnology and Biological Sciences Research Council BB/L021633/1
6 · The paper itself

Abstract

Alcohol oxidases, including carbohydrate oxidases, have a long history of research that has generated fundamental biological understanding and biotechnological applications. Despite a long history of study, the galactose 6-oxidase/glyoxal oxidase family of mononuclear copper-radical oxidases, Auxiliary Activity Family 5 (AA5), is currently represented by only very few characterized members. Here we report the recombinant production and detailed structure-function analyses of two homologues from the phytopathogenic fungi Colletotrichum graminicola and C. gloeosporioides, CgrAlcOx and CglAlcOx, respectively, to explore the wider biocatalytic potential in AA5. EPR spectroscopy and crystallographic analysis confirm a common active-site structure vis-à-vis the archetypal galactose 6-oxidase from Fusarium graminearum. Strikingly, however, CgrAlcOx and CglAlcOx are essentially incapable of oxidizing galactose and galactosides, but instead efficiently catalyse the oxidation of diverse aliphatic alcohols. The results highlight the significant potential of prospecting the evolutionary diversity of AA5 to reveal novel enzyme specificities, thereby informing both biology and applications.

Indexed as

Alcohol OxidoreductasesAlcoholsCatalytic DomainColletotrichumCrystallizationCrystallography, X-RayElectron Spin Resonance SpectroscopyFungal ProteinsFusariumGalactose OxidaseMutagenesis, Site-DirectedPhylogenyPichiaProtein Structure, SecondaryProtein Structure, TertiaryProton Magnetic Resonance Spectroscopyalcohol oxidaseAlcohol OxidoreductasesAlcoholsFungal ProteinsGalactose Oxidaseglyoxal oxidaseRecombinant Proteins

Identifiers

PMID26680532
PMCPMC4703870
OpenAlexW2254917337

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.