N-Acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N- acetylneuraminyl)-D-galactosyl-D-glucosylceramide
2,3-Didehydro-2-deoxysialic acids structurally varied at C-5 and their behaviour towards the sialidase from Vibrio cholerae.
CHARACTERIZATION, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Purification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2.
A kinetic-isotope-effect study of catalysis by Vibrio cholerae neuraminidase.
Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain.
Sialidases: structures, biological significance and therapeutic potential.
Investigation of the stability of thiosialosides toward hydrolysis by sialidases using NMR spectroscopy.
Multivalency and the mode of action of bacterial sialidases.
Sialic acid recognition by Vibrio cholerae neuraminidase.
Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase.
Characterization of Vibrio cholerae neuraminidase by a novel mechanism-based fluorescent labeling reagent.
This enzyme belongs to the glycosidase family-33. This enzyme is composed of three domains. The central catalytic domain is flanked by two lectin-like domains. The catalytic domain of this enzyme is homologous to other glycosidase family-33 neuramidases (T00065 in EzCatDB). Although this enzyme binds two calcium ions, they are not involved in catalysis. Since the active site of this enzyme is conserved and the same as that of its homologous enzyme, sialidase from Micromonospora viridifaciens (T00065 in EzCatDB), the catalytic mechanism of this enzyme is the same as that of the homologous enzyme. Asp250 acts as a general acid-base, whilst Tyr740 acts as a nucleophile.