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Sialidase

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'''Sialidase''' is a neuraminidase which cleaves terminal sialic acid from a variety of natural substances <ref>PMID:12374200</ref>. The sialic acid-binding domain of sialidase is called CBD. For '''Anhydrosialidase''' catalyzes the elimination of sialyl group in N-acetylneuraminic acid glycosides to yield 2,7-anhydro-α-N-acetylneuraminate. For '''Trans-sialidase''' see [[Neuraminidase]].
'''Sialidase''' is a neuraminidase which cleaves terminal sialic acid from a variety of natural substances <ref>PMID:12374200</ref>. The sialic acid-binding domain of sialidase is called CBD. For '''Anhydrosialidase''' catalyzes the elimination of sialyl group in N-acetylneuraminic acid glycosides to yield 2,7-anhydro-α-N-acetylneuraminate. For '''Trans-sialidase''' see [[Neuraminidase]].
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== Disease ==
 
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== Relevance ==
 
== Structural highlights ==
== Structural highlights ==

Revision as of 09:29, 11 November 2018

Sialidase complex with sialic acid (PDB code 3h72)

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3D structures of salidase

Updated on 11-November-2018

References

  1. Monti E, Preti A, Venerando B, Borsani G. Recent development in mammalian sialidase molecular biology. Neurochem Res. 2002 Aug;27(7-8):649-63. PMID:12374200
  2. Hsiao YS, Parker D, Ratner AJ, Prince A, Tong L. Crystal structures of respiratory pathogen neuraminidases. Biochem Biophys Res Commun. 2009 Mar 13;380(3):467-71. Epub 2009 Jan 23. PMID:19284989 doi:http://dx.doi.org/10.1016/j.bbrc.2009.01.108

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