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

TY - JOUR

T1 - Structure–function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family

AU - Yin, Delu Tyler

AU - Urresti, Saioa

AU - Lafond, Mickael

AU - Johnston, Esther M.

AU - Derikvand, Fatemeh

AU - Ciano, Luisa

AU - Berrin, Jean Guy

AU - Henrissat, Bernard

AU - Walton, Paul H.

AU - Davies, Gideon J.

AU - Brumer, Harry

PY - 2015/12/18

Y1 - 2015/12/18

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84950349925&partnerID=8YFLogxK

U2 - 10.1038/ncomms10197

DO - 10.1038/ncomms10197

M3 - Article

AN - SCOPUS:84950349925

SN - 2041-1723

VL - 6

JO - Nature Communications

JF - Nature Communications

M1 - 10197

ER -