Endo-α-sialidase

Endo-α-sialidase is an enzyme that catalyzes the hydrolysis of internal (2→8)-α-sialosyl linkages in oligosaccharide and polysaccharide substrates, particularly in polysialic acid chains[2]. Unlike exo-sialidases which remove terminal sialic acids from complex carbohydrates, endo-α-sialidases cleave linkages within sialic acid macromolecules[5]. The enzyme plays a significant role in bacterial pathogenesis, where sialidases broadly contribute to infection processes and bacterial colonization by modifying host glycoprotein and glycolipid substrates[3][4]. As a member of the sialidase enzyme family, endo-α-sialidase represents a potential therapeutic target for infections where bacterial sialidase activity facilitates disease pathogenesis, though specific drugs targeting this enzyme have not been identified in current literature.

Other names

N-acetylneuraminidasePoly(α-2,8-sialoside) α-2,8-sialosylhydrolaseEndosialidaseEndo-N

No specific drugs targeting endo-α-sialidase are identified in the provided search results, therefore no specific mechanism of action for such drugs is available.