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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

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