Neuraminidase

exo-α-sialidase
Identifiers
EC no.3.2.1.18
CAS no.9001-67-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Neuraminidase (GH34) ribbon diagram. An analog of its neuraminic acid substrate, used as an inhibitor drug, is the small white and red molecule in the center.
N-Acetylneuraminic acid

Exo-α-sialidase (EC 3.2.1.18, sialidase, neuraminidase; systematic name acetylneuraminyl hydrolase) is a glycoside hydrolase that cleaves the glycosidic linkages of neuraminic acids:

Hydrolysis of α-(2→3)-, α-(2→6)-, α-(2→8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates

Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. Viral neuraminidase was the first neuraminidase to be identified. It was discovered in 1957 by Alfred Gottschalk at the Walter and Eliza Hall Institute in Melbourne.[1] The viral neuraminidases are frequently used as antigenic determinants found on the surface of the influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologues are found in mammalian cells, which have a range of functions. At least four mammalian sialidase homologues have been described in the human genome (see NEU1, NEU2, NEU3, NEU4). Sialidases may act as pathogenic factors in microbial infections.[2]

  1. ^ "WEHI History: 1957 Discovery of Neuraminidase - Key Flu Molecule". WEHI. Retrieved 2023-11-08.
  2. ^ Rothe B, Rothe B, Roggentin P, Schauer R (April 1991). "The sialidase gene from Clostridium septicum: cloning, sequencing, expression in Escherichia coli and identification of conserved sequences in sialidases and other proteins". Molecular & General Genetics. 226 (1–2): 190–7. doi:10.1007/BF00273603. PMID 2034213. S2CID 21308462.