Kinetic parameters

Tree Display

AceDB Schema

XML Display


Mutation Report for: A328F_human-BCHE

Mode of mutation|Site directed mutagenesis
Amino Acid change|A328F
Torpedo number|330
Comment|p.A328F Ala328Phe (p.A356F Ala356Phe in primary sequence with 28 amino-acids signal peptide) Substrate activation; Aricept~Donepezil~E2020 inhibition;10-fold increase Ki vs WT
Kinetic parameters|none

    Title: The role of Phe329 in binding of cationic triarylmethane dyes to human butyrylcholinesterase
    Biberoglu K, Tacal O, Akbulut H
    Ref: Archives of Biochemistry & Biophysics, 511:64, 2011 : PubMed


    Title: Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept) to cholinesterases
    Saxena A, Fedorko JM, Vinayaka CR, Medhekar R, Radic Z, Taylor P, Lockridge O, Doctor BP
    Ref: European Journal of Biochemistry, 270:4447, 2003 : PubMed


    Title: Effects of mutations of active site residues and amino acids interacting with the Omega loop on substrate activation of butyrylcholinesterase
    Masson P, Xie W, Froment MT, Lockridge O
    Ref: Biochimica & Biophysica Acta, 1544:166, 2001 : PubMed


    Title: Differences in active-site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase
    Saxena A, Redman AM, Jiang X, Lockridge O, Doctor BP
    Ref: Chemico-Biological Interactions, 119-120:61, 1999 : PubMed


Send your questions or comments to :
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.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page

Acknowledgements and disclaimer