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Literature summary for 3.1.1.7 extracted from

  • Cheng, Y.H.; Cheng, X.L.; Radi?, Z.; McCammon, J.A.
    Acetylcholinesterase: mechanisms of covalent inhibition of H447I mutant determined by computational analyses (2008), Chem. Biol. Interact., 175, 196-199.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.7

Protein Variants

Protein Variants Comment Organism
H447I inhibitor TFK+ binding to the H447I mutant proceeds with a different reaction mechanism from the wild-type enzyme. A water molecule takes over the role of His447 and participates in the bond breaking and forming as a charge relayer. Unlike in the wild-type mAChE case, Glu334, a conserved residue from the catalytic triad, acts as a catalytic base in the reaction Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
TFK+ analysis of the inhibition mechanism by ab initio quantum mechanical/molecular mechanical approach and classical molecular dynamics simulations, overview Mus musculus
TFK0 analysis of the inhibition mechanism by ab initio quantum mechanical/molecular mechanical approach and classical molecular dynamics simulations, overview Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus P21836
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Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
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 additional information inhibition kinetics of wild-type and knockout mutant enzyme Mus musculus