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.