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

N-Acetylneuraminate lyase is the first committed enzyme in the degradation of sialic acid by bacterial pathogens. The kinetic parameters of MRSA N-acetylneuraminate lyase are reported and given a K_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 N-acetylneuraminate lyase enzymes, is a stronger inhibitor for MRSA N-acetylneuraminate lyase than Clostridium perfringens N-acetylneuraminate lyase. The crystal structure of ligand free and inhibitor bound MRSA N-acetylneuraminate lyase is presented. Subtle dynamic differences in solution and/or altered binding interactions within the active site may account for species-specific inhibition.