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

Filip Mollerup, Ville Aumala, Kirsti Parikka, Yann Mathieu, Harry Brumer, Maija Tenkanen, Emma Master*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

3 Citations (Scopus)
126 Downloads (Pure)

Abstract

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.

Original languageEnglish
Article numbere0216546
JournalPloS one
Volume14
Issue number5
DOIs
Publication statusPublished - 1 May 2019
MoE publication typeA1 Journal article-refereed

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