Y133A_human-ACHE

General

Gene Locus : human-ACHE

Mode of mutation : Site directed mutagenesis

Disease :

Summary : Choline binding site\;Catalysis\/Maintenance of Choline binding site 90 fold increase of Km for ATCh 760 fold red of kapp\;Ordentlich_1995_J.Biol.Chem_270_2082

AAA Change :

Allelic Variant :

Risk Factor :

Inhibitor :

Structure :

Disease by interaction :

Interact Gene Locus :

Xenobiotic sensitivity :

Modification : Choline binding site

Torpedo_number : 130

Kinetic Parameter : Acetylthiocholine_Y133A_human-ACHE, 3,3-dimethylbutylthioacetate_Y133A_human-ACHE, Edrophonium_Y133A_human-ACHE, Propidium_Y133A_human-ACHE, Decamethonium_Y133A_human-ACHE, Tacrine_Y133A_human-ACHE, HuperzineA_Y133A_human-ACHE

News : No news

Comment : "p.Y133A Tyr133Ala (p.Y164A Tyr164Ala in primary sequence with 31 amino-acids signal peptide) Choline binding site\;Catalysis\/Maintenance of Choline binding site 90 fold increase of Km for ATCh 760 fold red of kapp"

References (2)

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