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Hael, Jordi van Gestel, Hera Vlamakis, Colette Cywes-Bentley, Juan R. Computational and Structural Biotechnology Journal 2020, 18, 3324-3334. The staphylococcal exopolysaccharide PIA – Biosynthesis and role in biofilm formation, colonization, and infection. Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation. Staphylococcal Biofilms: Challenges and Novel Therapeutic Perspectives.
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Steady-state kinetic analysis reveals the low catalytic efficiency (pentasaccharide k cat/ K M 0.03 M –1 s –1) of the enzyme toward the oligomeric substrates.
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IcaB demonstrates metal-dependent de- N-acetylase activity on β-1,6-linked N-acetylglucosamine oligomers with a broad preference for divalent metals. To understand the mechanism of action of IcaB, the enzyme was overexpressed and purified. In Staphyloccocus epidermidis, the poly- N-acetylglucosamine polymer is partially de- N-acetylated by the extracellular protein IcaB. A polymer of partially de- N-acetylated β-1,6-linked N-acetylglucosamine (dPNAG), also known as the polysaccharide intercellular adhesin (PIA), is an important component of many bacterial biofilm matrices.