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Sialidases hydrolyse alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. Sialidases may act as pathogenic factors in microbial infections.[1]

Structure of trans-sialidase includes a catalytic beta-propeller domain, a N-terminal lectin-like domain and an irregular beta-stranded domain inserted into the catalytic domain.[2]

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  1. ^ Rothe B, Rothe B, Roggentin P, Schauer R (1991). "The sialidase gene from Clostridium septicum: cloning, sequencing, expression in Escherichia coli and identification of conserved sequences in sialidases and other proteins". Mol. Gen. Genet. 226 (1–2): 190–197. doi:10.1007/BF00273603. PMID 2034213.
  2. ^ Luo M, Luo Y, Li SC, Chou MY, Li YT (1998). "The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2-->3Gal specificity". Structure. 6 (4): 521–530. doi:10.1016/S0969-2126(98)00053-7. PMID 9562562.
This article incorporates text from the public domain Pfam and InterPro: IPR004124