Clostridium Perfringens Neuraminidase (NA) Protein

Clostridium Perfringens Neuraminidase (NA) Protein Products

Products	Source (CLICK for detailed Info. and Price)	Molecule	Description	Cat No
Protein	C. Perfringens Neuraminidase (NA), Recombinant Protein	NA	His Tag	11680-V07E

11680-V07E: The specific activity is 150,000 pmoles/min/µg. Measured by its ability to cleave a fluorogenic substrate, 2'-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic acid.

Clostridium Perfringens Neuraminidase (NA) Related Areas

Enzyme>>Carbohydrate Metabolism Enzymes>>Clostridium Perfringens Neuraminidase (NA)/Sialidase

Immunology>>Innate Immunity>>Lysosomal Enzyme>>Clostridium Perfringens Neuraminidase (NA)/Sialidase

Clostridium Perfringens Neuraminidase (NA) Alternative Names

Neuraminidase, NA, Sialidase, nanH

Clostridium Perfringens Neuraminidase (NA) Background

Neuraminidase enzymes are glycoside hydrolase enzymes which cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. Clostridium perfringens (formerly known as C. welchii) is a Gram-positive, rod-shaped, anaerobic, spore-forming bacterium of the genus Clostridium. C. perfringens is ubiquitous in nature and can be found as a normal component of decaying vegetation, marine sediment, the intestinal tract of humans and other vertebrates, insects, and soil. Bacterial neuraminidase is a virulence factor for many bacteria including Bacteroides fragilis and Pseudomonas aeruginosa, where it is produced to cleave a sialic acid residue off ganglioside-GM1 (a modulator of cell surface and receptor activity) turning it into asialo-GM1 to which its type 4 pilli (attachment factors) bind preferentially.

Clostridium Perfringens Neuraminidase, also called sialidases, catalyze the hydrolysis of terminal sialic acid residues from the newly formed virions and from the host cell receptors. Sialidase activities include assistance in the mobility of virus particles through the respiratory tract mucus and in the elution of virion progeny from the infected cell. Thus, Sialidases have been suggested to be pathogenic factors in microbial infections.

Clostridium Perfringens Neuraminidase (NA) Related Studies

Roggentin P, et al. (1988) Cloning and sequencing of a Clostridium perfringens sialidase gene. FEBS Lett. 238: 31-4.
Gaskell A, et al. (1995) The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll. Structure. 3: 1197-205.