10.6084/m9.figshare.5001938.v2 Rachel Aimee North Rachel Aimee North Andrew J A Watson Andrew J A Watson Grant Pearce Grant Pearce Andrew C Muscroft-Taylor Andrew C Muscroft-Taylor Rosmarie Friemann Rosmarie Friemann Antony J Fairbanks Antony J Fairbanks Renwick Dobson Renwick Dobson Dataset for: Structure and inhibition of <i>N</i>-acetylneuraminate lyase from methicillin-resistant <i>Staphylococcus aureus</i> Wiley 2017 Sialic acid degradation Drug discovery N-Acetylneuraminate lyase Biophysics Synthetic Biology Biochemistry Plant Biology Virology Receptors and Membrane Biology Computational Biology Immunology Neuroscience Cell Development, Proliferation and Death Molecular Biology Evolutionary Biology Signal Transduction Cancer Cell Biology Systems Biology Structural Biology 2017-06-20 07:07:21 Dataset https://wiley.figshare.com/articles/dataset/Dataset_for_Structure_and_inhibition_of_i_N_i_-acetylneuraminate_lyase_from_methicillin-resistant_i_Staphylococcus_aureus_i_/5001938 <i>N</i>-Acetylneuraminate lyase is the first committed enzyme in the degradation of sialic acid by bacterial pathogens. The kinetic parameters of MRSA <i>N</i>-acetylneuraminate lyase are reported and given a <i>K</i><sub>M</sub> of 3.2 mM, flux through the catabolic pathway is likely to be controlled by this enzyme. Sialic acid alditol, a known inhibitor of <i>N</i>-acetylneuraminate lyase enzymes, is a stronger inhibitor for MRSA <i>N</i>-acetylneuraminate lyase than <i>Clostridium perfringens N</i>-acetylneuraminate lyase. The crystal structure of ligand free and inhibitor bound MRSA <i>N</i>-acetylneuraminate lyase is presented. Subtle dynamic differences in solution and/or altered binding interactions within the active site may account for species-specific inhibition.