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Mutation Report for: PYGTP281-284EPYNGTA/G117H_human-BCHE

Mode of mutation|Site directed mutagenesis
Amino Acid change|
Torpedo number|283//284//285//286//287//119//119,283,284,285,286,287
Comment|computer simulation-driven strategy identified a surface peptide loop (residues 278-285) exhibiting dynamic motions during catalysis. The 3 amino acids insertions FVVPYGTP278-285FVVEPYNGTAP induced a slight but significant increase in reactivation of paraoxon inhibited enzyme
Kinetic parameters|none

    Title: Engineering Dynamic Surface Peptide Networks on ButyrylcholinesteraseG117H for Enhanced Organophosphosphorus Anticholinesterase Catalysis
    Hester KP, Bhattarai K, Jiang H, Agarwal PK, Pope C
    Ref: Chemical Research in Toxicology, 32:1801, 2019 : PubMed


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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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