Fig. 5: Effects of substrate length on the de-N-acetylation activity of Agd3. | Nature Communications

Fig. 5: Effects of substrate length on the de-N-acetylation activity of Agd3.

From: Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation

Fig. 5

a Time course of α-1,4-(GalNAc)8 de-N-acetylation by 1 µM Agd3 over 48 h. Enzymatic activity was monitored by MALDI-TOF MS of the m/z window 1500– 1800. The MS traces correspond to the following time points: 0, 1, 2, 3, 6, 24, and 48 h. b Time course of de-N-acetylation of GalNAc oligosaccharides ranging from pentamer to 16-mers. Signals from each oligosaccharide were integrated and graphed as the percentage of fully acetylated oligosaccharide over time. The degree of de-N-acetylation of each oligosaccharide is indicated by the color of the 3D surface.

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