Structural highlights
Function
NANA_STAA8 Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate (By similarity).
Publication Abstract from PubMed
N-Acetylneuraminate lyase is the first committed enzyme in the degradation of sialic acid by bacterial pathogens. In this study, we analyzed the kinetic parameters of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus (MRSA). We determined that the enzyme has a relatively high KM of 3.2 mm, suggesting that flux through the catabolic pathway is likely to be controlled by this enzyme. Our data indicate that sialic acid alditol, a known inhibitor of N-acetylneuraminate lyase enzymes, is a stronger inhibitor of MRSA N-acetylneuraminate lyase than of Clostridium perfringens N-acetylneuraminate lyase. Our analysis of the crystal structure of ligand-free and 2R-sialic acid alditol-bound MRSA N-acetylneuraminate lyase suggests that subtle dynamic differences in solution and/or altered binding interactions within the active site may account for species-specific inhibition.
Structure and inhibition of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus.,North RA, Watson AJ, Pearce FG, Muscroft-Taylor AC, Friemann R, Fairbanks AJ, Dobson RC FEBS Lett. 2016 Dec;590(23):4414-4428. doi: 10.1002/1873-3468.12462. Epub 2016, Nov 7. PMID:27943302[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ North RA, Watson AJ, Pearce FG, Muscroft-Taylor AC, Friemann R, Fairbanks AJ, Dobson RC. Structure and inhibition of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus. FEBS Lett. 2016 Dec;590(23):4414-4428. doi: 10.1002/1873-3468.12462. Epub 2016, Nov 7. PMID:27943302 doi:http://dx.doi.org/10.1002/1873-3468.12462
