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
| 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 |
| Abstract : Shafferman_2005_Chem.Biol.Interact_157-158_123 |
| ESTHER : Shafferman_2005_Chem.Biol.Interact_157-158_123 |
| PubMedSearch : Shafferman_2005_Chem.Biol.Interact_157-158_123 |
| 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 |
| Abstract : Shafferman_1992_J.Biol.Chem_267_17640 |
| ESTHER : Shafferman_1992_J.Biol.Chem_267_17640 |
| PubMedSearch : Shafferman_1992_J.Biol.Chem_267_17640 |
| PubMedID: 1517212 |