Endosialidases: Versatile Tools for the Study of Polysialic Acid.

摘要: Polysialic acid is an α2,8-linked N-acetylneuraminic polymer found on the surface of both bacterial and eukaryotic cells. Endosialidases are bacteriophage-borne glycosyl hydrolases that specifically cleave polysialic acid. The crystal structure endosialidase reveals a trimeric mushroom-shaped molecule which, in addition to active site, harbors two additional binding sites. Folding protein crucially depends intramolecular C-terminal chaperone domain proteolytically released reaction. Based structural data previous considerations, updated catalytic mechanism discussed. degrade processive mode action, model for its suggested. review summarizes biochemical elucidations last decade importance endosialidases medical applications. Active important tools studies biological roles acid, such as pathogenesis septicemia meningitis by acid-encapsulated bacteria, or role modulator adhesion interactions neural other Endosialidase mutants have lost their cleaving activity while retaining capability been fused green fluorescent provide efficient tool specific detection