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Literature summary for 3.2.1.18 extracted from

  • Raab, M.; Tvaroska, I.
    The binding properties of the H5N1 influenza virus neuraminidase as inferred from molecular modeling (2011), J. Mol. Model., 17, 1445-1456.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
influenza A virus
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avian influenzy virus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate specificity of the viral enzyme with sialic acid, methyl 3'-sialyllactoside, methyl 6'-sialyllactoside, ligand conformations, enzyme-ligand interactions, and loop flexibility, analyzed by molecular docking and molecular dynamics simulations, and molecular modeling, overview. Methyl 3'-sialyllactoside has only weak interactions with the 150-loop, whereas the enzyme N1-methyl 6'-sialyllactoside complex shows strong interactions. The avian neuraminidase N1 preferentially cleaves sialic acid from alpha-(2-3)-Gal glycoconjugates over alpha-(2-6)-Gal, also due to the altered flexibility of loops in and around the active site influenza A virus ?
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Synonyms

Synonyms Comment Organism
neuraminidase
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influenza A virus