2 research outputs found
New insights on the features of the vinyl phenol reductase from the wine-spoilage yeast Dekkera/Brettanomyces bruxellensis
Vinyl phenol reductase activity was assayed in
extracts from 19 strains of Dekkera bruxellensis isolated from
wine. In all strains, vinyl phenol reductase activity was insensitive
to the presence/absence of 4-vinyl guaiacol, confirming
that expression is not related to the presence of the substrate.
D. bruxellensis CBS 4481 showed the highest vinyl phenol
reductase activity toward 4-vinyl guaiacol. Vinyl phenol reductase
from D. bruxellensis CBS 4481 was purified to mass
spectrometric homogeneity, and sequenced by trypsinolysis
and mass spectrometry. The sequence of the purified protein
showed convincing homology with a Cu/Zn superoxide dismutase
in the D. bruxellensisAWRI 1499 genome, and indeed
it was found to possess both vinyl phenol reductase and
superoxide dismutase activities. A bioinformatics analysis of
the sequence of vinyl phenol reductase/superoxide dismutase
from D. bruxellensis CBS 4481 reveals the presence in this
protein of cofactor-binding structural features, that are
absent in sequences of superoxide dismutases from related
microorganisms, that do not display vinyl phenol reductase
activity