E334D_human-ACHE

General

Gene Locus : human-ACHE

Mode of mutation : Site directed mutagenesis

Disease :

Summary : Catalysis No activity Shafferman_1992_J.Biol.Chem_267_17640 Shafferman_1992_EMBO.J_11_3561 Shafferman_2005_Chem.Biol.Interact_157-158_123 || Catalytic triad No activity Shafferman_1992_J.Biol.Chem_267_17640 Shafferman_1992_EMBO.J_11_3561 Shafferman_2005_Chem.Biol.Interact_157-158_123

AAA Change :

Allelic Variant :

Risk Factor :

Inhibitor :

Structure :

Disease by interaction :

Interact Gene Locus :

Xenobiotic sensitivity :

Modification : Catalytic triad || Catalysis

Torpedo_number : 327

Kinetic Parameter : No kinetic parameter

News : No news

Comment :
p.E334D Glu334Asp (p.E365D Glu365Asp in primary sequence with 31 amino-acids signal peptide) Catalytic triad Catalysis\;No activity

References (2)

Title : Functional requirements for the optimal catalytic configuration of the AChE active center - Shafferman_2005_Chem.Biol.Interact_157-158_123
Author(s) : Shafferman A , Barak D , Kaplan D , Ordentlich A , Kronman C , Velan B
Ref : Chemico-Biological Interactions , 157-158 :123 , 2005
PubMedID: 16256968

Title : Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding - Shafferman_1992_J.Biol.Chem_267_17640
Author(s) : Shafferman A , Kronman C , Flashner Y , Leitner M , Grosfeld H , Ordentlich A , Gozes Y , Cohen S , Ariel N , Barak D , Harel M , Silman I , Sussman JL , Velan B
Ref : Journal of Biological Chemistry , 267 :17640 , 1992
PubMedID: 1517212