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Mutation Report for: I365C/D413C_drome-ACHE

Mode of mutation|Site directed mutagenesis
Amino Acid change|I365C/D413C
Torpedo number|287,335//287//335
Comment|Seven mutations made to create dissulfide bond and increase stability. Two decreased production, and only one increased stability (I327C/D375C). The numbering in the paper is for the mature enzyme R24C/A169C (R62C/A207C; TorNum: 25/138), I327C/D375C (I365C/D413C; TorNum: 287/335), L354C/A456C (L392C/A494C; TorNum: 314/416), T369C/M476C (T407C/M514C; TorNum: 329/436), L388C/Q427C (L426C/Q464C; TorNum: 347/386), A452C/S533C (A490C/S571C; TorNum: 412/496), T464C/S543C (T502C/S581C; TorNum: 424/506)
Kinetic parameters|none

    Title: The effect of engineered disulfide bonds on the stability of Drosophila melanogaster acetylcholinesterase
    Siadat OR, Lougarre A, Lamouroux L, Ladurantie C, Fournier D
    Ref: BMC Biochem, 7:12, 2006 : 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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