File:Project description.docx

Certain carbohydrate esterase family 4 (CE4) enzymes show metal-dependent ¬de-N¬-acetylation of various different polymers of GlcNAc including chitin, peptidoglycan, and polysaccharide-intracellular-adhesin (PIA). The activity of these de-N-acetylation enzymes results in the continuing pathogenicity of the respective organisms. This makes the de-N-acetylatases attractive antibiotic targets. The crystal structures of these de-N-acetylatases revealed a difference in the size of the acyl binding pockets, proximal to the catalytic centre, across the various enzymes. Exploiting the difference in the acyl binding pockets, the substrate specificity of these enzymes was called into question. Employing a fluorescamine-based assay the substrate specificity of these de-N¬-acetylation enzymes using monosaccharide benzyl glycosides with diverse acyl groups will be presented.