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

Filip Mollerup, Ville Aumala, Kirsti Maria Parikka, Yan Mathieu, Harry Brumer, Tiina Maija Tenkanen, Emma Master

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

Sammanfattning

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.

Originalspråkengelska
Artikelnummer0216546
TidskriftPLoS One
Volym14
Nummer5
Sidor (från-till)1-19
Antal sidor19
ISSN1932-6203
DOI
StatusPublicerad - 15 maj 2019
MoE-publikationstypA1 Tidskriftsartikel-refererad

Vetenskapsgrenar

  • 414 Jordbruksbioteknologi
  • 1183 Växtbiologi, mikrobiologi, virologi

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