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A rapid quantitative activity assay shows that the Vibrio cholerae colonization factor GbpA is an active lytic polysaccharide monooxygenase
Author(s) -
Loose Jennifer S.M.,
Forsberg Zarah,
Fraaije Marco W.,
Eijsink Vincent G.H.,
Vaaje-Kolstad Gustav
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.07.036
Subject(s) - lytic cycle , polysaccharide , microbiology and biotechnology , virulence factor , biology , vibrio cholerae , monooxygenase , bacteria , enzyme , virulence , chemistry , biochemistry , virology , cytochrome p450 , virus , genetics , gene
The discovery of the copper‐dependent lytic polysaccharide monooxygenases (LPMOs) has revealed new territory for chemical and biochemical analysis. These unique mononuclear copper enzymes are abundant, suggesting functional diversity beyond their established roles in the depolymerization of biomass polysaccharides. At the same time basic biochemical methods for characterizing LPMOs, such as activity assays are not well developed. Here we describe a method for quantification of C1‐oxidized chitooligosaccharides (aldonic acids), and hence LPMO activity. The method was used to quantify the activity of a four‐domain LPMO from Vibrio cholerae , GbpA, which is a virulence factor with no obvious role in biomass processing.