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

Author

Listed:
  • DeLu (Tyler) Yin

    (University of British Columbia)

  • Saioa Urresti

    (University of York)

  • Mickael Lafond

    (University of British Columbia
    Institut des Sciences Moléculaires de Marseille—Team BiosCiences UMR 7313-CNRS, Aix-Marseille University)

  • 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
    INRA, USC 1408 AFMB
    King Abdulaziz University)

  • Paul H. Walton

    (University of York)

  • Gideon J. Davies

    (University of York)

  • Harry Brumer

    (University of British Columbia)

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.

Suggested Citation

  • 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 & Harry Brumer, 2015. "Structure–function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family," Nature Communications, Nature, vol. 6(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms10197
    DOI: 10.1038/ncomms10197
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