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Mutation Report for: L286H_human-BCHE

L286H_human-BCHE
Gene_Locus|human-BCHE
Mode of mutation|Site directed mutagenesis
Amino Acid change|L286H
Torpedo number|288
Summary|
Comment|p.L286H Leu286His (p.L314H Leu314His in primary sequence with 28 amino-acids signal peptide) Phosphotriesterase activity Identical to WT. Tentative to place an Histidine in the active site at other place than the G117H mutation. Though the L286H mutant reactivated 400-fold more slowly than G117H, it was still 250-fold faster than wild-type BChE. Adjusting the position of histidine 286 by adding glycine residues to the sequence, e.g., L286GH, L286HG, and L286GHG, did not improve the reactivation rate
Kinetic parameters|none


References:
    Title: Mutants of human butyrylcholinesterase with organophosphate hydrolase activity; evidence that His117 is a general base catalyst for hydrolysis of echothiophate
    Schopfer LM, Boeck AT, Broomfield CA, Lockridge O
    Ref: Journal of Medicinal Chemistryical Biology Radiol Def, 2:1, 2004 : PubMed

            

    Title: A single amino acid substitution, Gly117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase
    Lockridge O, Blong RM, Masson P, Froment MT, Millard CB, Broomfield CA
    Ref: Biochemistry, 36:786, 1997 : 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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