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Mutation Report for: Y72A/E285A_human-ACHE

Y72A/E285A_human-ACHE
Gene_Locus|human-ACHE
Mode of mutation|Site directed mutagenesis
Amino Acid change|Y72A/E285A
Torpedo number|70,278//278//70
Summary|
Comment|p.Y72A/E285A Tyr72Ala/Glu285Ala (p.Y103A/E316A Tyr103Ala/Glu316Ala in primary sequence with 31 amino-acids signal peptide) Peripheral Anionic Site;Ki of PAS ligand increased >10X
Kinetic parameters|Acetylthiocholine_Y72A/E285A_human-ACHE,
BW284C51_Y72A/E285A_human-ACHE,
Decamethonium_Y72A/E285A_human-ACHE,
Edrophonium_Y72A/E285A_human-ACHE,
Hexamethonium_Y72A/E285A_human-ACHE,
Propidium_Y72A/E285A_human-ACHE


References:
    Title: Molecular Aspects of Catalysis and of Allosteric Regulation of Aceytlcholinesterases
    Shafferman A, Ordentlich A, Barak D, Kronman C, Ariel N, Leitner M, Segall Y, Bromberg A, Reuveny S and Velan B <4 more author(s)>
    Ref: In Enzyme of the Cholinesterase Family - Proceedings of Fifth International Meeting on Cholinesterases, (Quinn, D.M., Balasubramanian, A.S., Doctor, B.P., Taylor, P., Eds) Plenum Publishing Corp.:189, 1995 : PubMed

            

    Title: Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core
    Barak D, Kronman C, Ordentlich A, Ariel N, Bromberg A, Marcus D, Lazar A, Velan B, Shafferman A
    Ref: Journal of Biological Chemistry, 269:6296, 1994 : PubMed

            




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