EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.18 | 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 | |
3.2.1.18 | 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 | |
3.2.1.18 | 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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.18 | influenza A virus | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.18 | 2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid + H2O | - |
influenza A virus | 4-methylumbelliferone + alpha-D-N-acetylneuraminic acid | - |
? |