A family AA5_2 carbohydrate oxidase from Penicillium rubens displays functional overlap across the AA5 family

Copper radical alcohol oxidases belonging to auxiliary activity family 5, subfamily 2 (AA5_2) catalyze the oxidation of galactose and galactosides, as well as aliphatic alcohols. Despite their broad applied potential, so far very few AA5_2 members have been biochemically characterized. We report the recombinant production and biochemical characterization of an AA5_2 oxidase from Penicillium rubens Wisconsin 54–1255 (PruAA5_2A), which groups within an unmapped clade phylogenetically distant from those comprising AA5_2 members characterized to date. PruAA5_2 preferentially oxidized raffinose over galactose; however, its catalytic efficiency was 6.5 times higher on glycolaldehyde dimer compared to raffinose. Deep sequence analysis of characterized AA5_2 members highlighted amino acid pairs correlated to substrate range and conserved within the family. Moreover, PruAA5_2 activity spans substrate preferences previously reported for AA5 subfamily 1 and 2 members, identifying possible functional overlap across the AA5 family.

DOI

10.1371/journal.pone.0216546

Citation

Mollerup , F , Aumala , V , Parikka , K , Mathieu , Y , Brumer , H , Tenkanen , M & Master , E 2019 , ' A family AA5_2 carbohydrate oxidase from Penicillium rubens displays functional overlap across the AA5 family ' , PloS one , vol. 14 , no. 5 , e0216546 . https://doi.org/10.1371/journal.pone.0216546

Permanent link to this item

https://urn.fi/URN:NBN:fi:aalto-201906203940

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[article-cris] Kemian tekniikan korkeakoulu / CHEM

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