Gene Locus : human-ACHE
Mode of mutation : Site directed mutagenesis
Disease :
Summary : Omega loop interaction No effect Velan_1996_FEBS.Lett_395_22 || Peripheral Anionic Site low decrease in affinity for edrophonium, no inhib by excess substrate Shafferman_1992_EMBO.J_11_3561 Shafferman_1992_4th.ChE.Meeting.Eilat__165 Barak_1994_J.Biol.Chem_269_6296 Shafferman_1995_5th.ChE.Meeting.Madras__189 || oxime interaction reactivation of tabun-inhibited human AChE. The dissociation constant 3.5-fold increased Artursson_2009_Toxicology_265_108
AAA Change :
Allelic Variant :
Risk Factor :
Inhibitor :
Structure :
Disease by interaction :
Interact Gene Locus :
Xenobiotic sensitivity :
Modification : Peripheral Anionic Site || Omega loop interaction || Oxime interaction
Torpedo_number : 334
Kinetic Parameter : Acetylthiocholine_Y341A_human-ACHE, Edrophonium_Y341A_human-ACHE, Hexamethonium_Y341A_human-ACHE, BW284C51_Y341A_human-ACHE, Propidium_Y341A_human-ACHE, Decamethonium_Y341A_human-ACHE, Tacrine_Y341A_human-ACHE, HuperzineA_Y341A_human-ACHE
News : No news
Comment :
p.Y341A Tyr341Ala (p.Y372A Tyr372Ala in primary sequence with 31 amino-acids signal peptide) Omega loop interaction\;No effect - Peripheral Anionic Site\;low decrease in affinity for edrophonium, no inhib by excess substrate -oxime interaction\;reactivation of tabun-inhibited human AChE. The dissociation constant 3.5-fold increased
Title : Reactivation of tabun-hAChE investigated by structurally analogous oximes and mutagenesis - Artursson_2009_Toxicology_265_108 |
Author(s) : Artursson E , Akfur C , Hornberg A , Worek F , Ekstrom F |
Ref : Toxicology , 265 :108 , 2009 |
Abstract : |
PubMedSearch : Artursson_2009_Toxicology_265_108 |
PubMedID: 19761810 |
Title : The 'aromatic patch' of three proximal residues in the human acetylcholinesterase active centre allows for versatile interaction modes with inhibitors - Ariel_1998_Biochem.J_335_95 |
Author(s) : Ariel N , Ordentlich A , Barak D , Bino T , Velan B , Shafferman A |
Ref : Biochemical Journal , 335 :95 , 1998 |
Abstract : |
PubMedSearch : Ariel_1998_Biochem.J_335_95 |
PubMedID: 9742217 |
Title : Structural modifications of the omega loop in human acetylcholinesterase - Velan_1996_FEBS.Lett_395_22 |
Author(s) : Velan B , Barak D , Ariel N , Leitner M , Bino T , Ordentlich A , Shafferman A |
Ref : FEBS Letters , 395 :22 , 1996 |
Abstract : |
PubMedSearch : Velan_1996_FEBS.Lett_395_22 |
PubMedID: 8849682 |
Title : Molecular Aspects of Catalysis and of Allosteric Regulation of Aceytlcholinesterases - |
Author(s) : Shafferman A , Ordentlich A , Barak D , Kronman C , Ariel N , Leitner M , Segall Y , Bromberg A , Reuveny S , Marcus D , Bino T , Lazar A , Cohen S , Velan B |
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 |
PubMedID: |
Title : Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core - Barak_1994_J.Biol.Chem_269_6296 |
Author(s) : 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 |
Abstract : |
PubMedSearch : Barak_1994_J.Biol.Chem_269_6296 |
PubMedID: 8119978 |
Title : Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center - Shafferman_1992_EMBO.J_11_3561 |
Author(s) : Shafferman A , Velan B , Ordentlich A , Kronman C , Grosfeld H , Leitner M , Flashner Y , Cohen S , Barak D , Ariel N |
Ref : EMBO Journal , 11 :3561 , 1992 |
Abstract : |
PubMedSearch : Shafferman_1992_EMBO.J_11_3561 |
PubMedID: 1396557 |
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: |