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Literature summary for 3.4.21.75 extracted from

  • Guo, X.L.; Li, L.; Wei, D.Q.; Zhu, Y.S.; Chou, K.C.
    Cleavage mechanism of the H5N1 hemagglutinin by trypsin and furin (2008), Amino Acids, 35, 375-382.
    View publication on PubMed

Application

Application Comment Organism
medicine some mutations of H5N1 H5 cleavage sequence fit less well into furin and hence may reduce the high pathogenicity of the H5N1 virus Mus musculus

Crystallization (Commentary)

Crystallization (Comment) Organism
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Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
high pathogenic H5N1 hemagglutinin + H2O furin can only cleave the high pathogenic hemagglutinin. It generates most of its selectivity through interactions with subsites P1, P4, and P6, with interactions at P2 being less important and little preference at P3, P5, P7, and P8. The S1, S4, and S6 pockets are specifically designed to accommodate arginine, with lysine substitution fitting less well in different degrees Mus musculus ?
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additional information no cleavage of the low pathogenic H1N1 H1 hemagglutinin Mus musculus ?
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