Dataset for: Structure and inhibition of <i>N</i>-acetylneuraminate lyase from methicillin-resistant <i>Staphylococcus aureus</i>

<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>_M 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.