Article Metrics


Online attention

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

DOI: 10.1038/ncomms10197 DOI Help
PMID: 26680532 PMID Help

Authors: Delu (tyler) Yin (University of British Columbia) , Saioa Urresti (University of York) , Mickael Lafond (University of British Columbia) , Esther M. Johnston (University of York) , Fatemeh Derikvand (University of British Columbia) , Luisa Ciano (University of York) , Jean- Guy Berrin (INRA, UMR1163 Biodiversité et Biotechnologie Fongiques Marseille) , Bernard Henrissat (CNRS—Aix-Marseille University) , Paul Walton (University of York) , Gideon Davies (University of York) , Harry Brumer (University of British Columbia)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 6

State: Published (Approved)
Published: December 2015
Diamond Proposal Number(s): 9948

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-a-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.

Journal Keywords: Biological sciences Biochemistry

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Added On: 16/02/2016 11:21

Discipline Tags:

Technical Tags: