Literature summary for 3.2.1.18 extracted from

Tecle, T.; White, M.R.; Crouch, E.C.; Hartshorn, K.L.
Inhibition of influenza viral neuraminidase activity by collectins (2007), Arch. Virol., 152, 1731-1742.

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Inhibitors

Inhibitors	Comment	Organism	Structure
lung surfactant protein A	lung surfactant protein D has greater neuraminidase inhibitory activity than mannose-binding lectin, which in turn has greater activity than lung surfactant protein A	influenza A virus
lung surfactant protein D	neuraminidase inhibition by lung surfactant protein D correlates with binding of its carbohydrate recognition domain to oligomannose oligosaccharides on the viral hemagglutinin. The effects of lung surfactant protein D are additive with oseltamivir. Neuraminidase inhibition is observed using fetuin or MDCK cells as a substrate, but not in assays using a soluble sialic acid analogue. Lung surfactant protein D has greater neuraminidase inhibitory activity than mannose-binding lectin, which in turn has greater activity than lung surfactant protein A	influenza A virus
mannose-binding lectin	lung surfactant protein D has greater neuraminidase inhibitory activity than mannose-binding lectin, which in turn has greater activity than lung surfactant protein A	influenza A virus

Organism

Organism	UniProt	Comment	Textmining
influenza A virus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O	-	influenza A virus	4-methylumbelliferone + alpha-D-N-acetylneuraminic acid	-	?

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Release 2023.1 (January 2023)