A family AA5_2 carbohydrate oxidase from Penicillium rubens displays functional overlap across the AA5 family
Loading...
Access rights
openAccess
publishedVersion
URL
Journal Title
Journal ISSN
Volume Title
A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
This publication is imported from Aalto University research portal.
View publication in the Research portal (opens in new window)
View/Open full text file from the Research portal (opens in new window)
View publication in the Research portal (opens in new window)
View/Open full text file from the Research portal (opens in new window)
Date
Department
Major/Subject
Mcode
Degree programme
Language
en
Pages
19
Series
PloS One, Volume 14, issue 5
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.Description
Keywords
Other note
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