Gene Locus : human-ACHE
Mode of mutation : Site directed mutagenesis
Disease :
Summary : Folding\;Non producer\;Shafferman_1992_J.Biol.Chem_267_17640\;Shafferman_1992_4th.ChE.Meeting.Eilat__165 || Salt bridge\;Non producer\;Shafferman_1992_J.Biol.Chem_267_17640\;Shafferman_1992_4th.ChE.Meeting.Eilat__165
AAA Change :
Allelic Variant :
Risk Factor :
Inhibitor :
Structure :
Disease by interaction :
Interact Gene Locus :
Xenobiotic sensitivity :
Modification : Folding || Salt bridge
Torpedo_number : 172
Kinetic Parameter : No kinetic parameter
News : No news
Comment : p.D175N Asp175Asn (p.D206N Asp206Asn in primary sequence with 31 amino-acids signal peptide) Non producer Folding Salt bridge
| Title : Acetylcholinesterase Catalysis - Protein Engineering Studies - |
| Author(s) : Shafferman A , Velan B |
| Ref : In Multidisciplinary approaches to cholinesterase functions - Proceedings of Fourth International Meeting on Cholinesterases , (Shafferman, A. and Velan, B., Eds) Plenum Press, New York :165 , 1992 |
| PubMedID: |
| 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 |