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Mutation Report for: F295L/F297V/Y337A_human-ACHE

F295L/F297V/Y337A_human-ACHE
Gene_Locus|human-ACHE
Mode of mutation|Site directed mutagenesis
Amino Acid change|F295L/F297V/Y337A
Torpedo number|288//290//330//288,290,330
Summary|
Comment|p.F295L/F297V/Y337A Phe295Leu/Phe297Val/Tyr337Ala (p.F326L/F328V/Y368A Phe326Leu/Phe328Val/Tyr368Ala in primary sequence with 31 amino-acids signal peptide) Acyl specificity;replacement of aromatic active center residues in human-ACHE by the corresponding residues in human-BCHE
Kinetic parameters|Acetylthiocholine_F295L/F297V/Y337A_human-ACHE,
Butyrylthiocholine_F295L/F297V/Y337A_human-ACHE,
Decamethonium_Y72N/Y124Q/W286A_human-ACHE,
Edrophonium_F295L/F297V/Y337A_human-ACHE,
HuperzineA_F295L/F297V/Y337A_human-ACHE,
Tacrine_F295L/F297V/Y337A_human-ACHE


References:
    Title: Lessons from functional analysis of AChE covalent and noncovalent inhibitors for design of AD therapeutic agents
    Barak D, Ordentlich A, Kaplan D, Kronman C, Velan B, Shafferman A
    Ref: Chemico-Biological Interactions, 157-158:219, 2005 : PubMed

            

    Title: Does butyrylization of acetylcholinesterase through substitution of the six divergent aromatic amino acids in the active center gorge generate an enzyme mimic of butyrylcholinesterase?
    Kaplan D, Ordentlich A, Barak D, Ariel N, Kronman C, Velan B, Shafferman A
    Ref: Biochemistry, 40:7433, 2001 : PubMed

            




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