Y337F_human-ACHE

General

Gene Locus : human-ACHE

Mode of mutation : Site directed mutagenesis

Disease :

Summary : Signal transduction very low effect on catalysis and inhibition Shafferman_1992_EMBO.J_11_3561 Shafferman_1992_4th.ChE.Meeting.Eilat__165 Ordentlich_1993_J.Biol.Chem_268_17083 Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097 Ashani_1994_Mol.Pharmacol_45_555 Barak_1994_J.Biol.Chem_269_6296 Ordentlich_1995_J.Biol.Chem_270_2082 || Substrate inhibition identical to wild type Shafferman_1992_EMBO.J_11_3561 Shafferman_1992_4th.ChE.Meeting.Eilat__165 Ordentlich_1993_J.Biol.Chem_268_17083 Shafferman_1993_Proc.Med.Def.Biosci.Rev_3_1097 Ashani_1994_Mol.Pharmacol_45_555 Barak_1994_J.Biol.Chem_269_6296 Ordentlich_1995_J.Biol.Chem_270_2082 || oxime interaction reactivation of tabun-inhibited human AChE. Unable to facilitate HI-6-mediated reactivation of tabun-hAChE. Induced a 2-2.5-fold enhancement of the bimolecular rate constant for K027 and HLo-7 Artursson_2009_Toxicology_265_108

AAA Change :

Allelic Variant :

Risk Factor :

Inhibitor :

Structure :

Disease by interaction :

Interact Gene Locus :

Xenobiotic sensitivity :

Modification : Signal transduction || Substrate inhibition || Oxime interaction

Torpedo_number : 330

Kinetic Parameter : Acetylthiocholine_Y337F_human-ACHE, Edrophonium_Y337F_human-ACHE, Hexamethonium_Y337F_human-ACHE, BW284C51_Y337F_human-ACHE, Propidium_Y337F_human-ACHE, Decamethonium_Y337F_human-ACHE, 3,3-dimethylbutylthioacetate_Y337F_human-ACHE, Tacrine_Y337F_human-ACHE, HuperzineA_Y337F_human-ACHE

News : No news

Comment : p.Y337F Tyr337Phe (p.Y368F Tyr368Phe in primary sequence with 31 amino-acids signal peptide) Signal transduction, very low effect on catalysis and inhibition\; Substrate inhibition identical to wild type

References (9)

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 : Artursson_2009_Toxicology_265_108
ESTHER : Artursson_2009_Toxicology_265_108
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 : Ariel_1998_Biochem.J_335_95
ESTHER : Ariel_1998_Biochem.J_335_95
PubMedSearch : Ariel_1998_Biochem.J_335_95
PubMedID: 9742217

Title : Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase - Ordentlich_1995_J.Biol.Chem_270_2082
Author(s) : Ordentlich A , Barak D , Kronman C , Ariel N , Segall Y , Velan B , Shafferman A
Ref : Journal of Biological Chemistry , 270 :2082 , 1995
Abstract : Ordentlich_1995_J.Biol.Chem_270_2082
ESTHER : Ordentlich_1995_J.Biol.Chem_270_2082
PubMedSearch : Ordentlich_1995_J.Biol.Chem_270_2082
PubMedID: 7836436

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 : Barak_1994_J.Biol.Chem_269_6296
ESTHER : Barak_1994_J.Biol.Chem_269_6296
PubMedSearch : Barak_1994_J.Biol.Chem_269_6296
PubMedID: 8119978

Title : Role of tyrosine 337 in the binding of huperzine A to the active site of human acetylcholinesterase - Ashani_1994_Mol.Pharmacol_45_555
Author(s) : Ashani Y , Grunwald J , Kronman C , Velan B , Shafferman A
Ref : Molecular Pharmacology , 45 :555 , 1994
Abstract : Ashani_1994_Mol.Pharmacol_45_555
ESTHER : Ashani_1994_Mol.Pharmacol_45_555
PubMedSearch : Ashani_1994_Mol.Pharmacol_45_555
PubMedID: 8145739
Gene_locus related to this paper: human-ACHE

Title : Recombinant human acetylcholinesterase - Enzyme engineering -
Author(s) : Shafferman A , Velan B , Barak D , Kronman C , Ordentlich A , Flashner Y , Leitner M , Segal Y , Grosfeld H , Stein D , Ariel N
Ref : Medical Defense Bioscience Review , 3 :1097 , 1993
PubMedID:

Title : Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocket - Ordentlich_1993_J.Biol.Chem_268_17083
Author(s) : Ordentlich A , Barak D , Kronman C , Flashner Y , Leitner M , Segall Y , Ariel N , Cohen S , Velan B , Shafferman A
Ref : Journal of Biological Chemistry , 268 :17083 , 1993
Abstract : Ordentlich_1993_J.Biol.Chem_268_17083
ESTHER : Ordentlich_1993_J.Biol.Chem_268_17083
PubMedSearch : Ordentlich_1993_J.Biol.Chem_268_17083
PubMedID: 8349597
Gene_locus related to this paper: human-ACHE , human-BCHE

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 : Shafferman_1992_EMBO.J_11_3561
ESTHER : Shafferman_1992_EMBO.J_11_3561
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: