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 Harry Brumer ()
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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
Bernard Henrissat: Architecture et Fonction des Macromolécules Biologiques, CNRS—Aix-Marseille University
Paul H. Walton: University of York
Gideon J. Davies: University of York
Harry Brumer: University of British Columbia

Nature Communications, 2015, vol. 6, issue 1, 1-13

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms10197

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