A328Y_human-BCHE

General

Gene Locus : human-BCHE

Mode of mutation : Site directed mutagenesis

Disease :

Summary : Cocaine hydrolysis 4-fold improvement in catalytic efficiency kcat\/Km Xie_1999_Mol.Pharmacol_55_83 || Binding of inhibitors smaller dimension of the active-site gorge Saxena_1999_Chem.Biol.Interact_119-120_61 || Substrate activation substrate activation Masson_2001_Biochim.Biophys.Acta_1544_166 || Aricept~Donepezil~E2020 inhibition small increase Ki vs WT Saxena_2003_Eur.J.Biochem_270_4447

AAA Change :

Allelic Variant :

Risk Factor :

Inhibitor :

Structure :

Disease by interaction :

Interact Gene Locus :

Xenobiotic sensitivity :

Modification : Acyl specificity || Substrate activation || Cocaine hydrolysis || Aricept~Donepezil~E2020 inhibition

Torpedo_number : 330

Kinetic Parameter : No kinetic parameter

News : No news

Comment : p.A328Y Ala328Tyr (p.A356Y Ala356Tyr in primary sequence with 28 amino-acids signal peptide)Cocaine hydrolysis\;4-fold improvement in catalytic efficiency kcat\/Km Substrate activation, Aricept~Donepezil~E2020 inhibition\;small increase Ki vs WT

References (6)

Title : Probing the peripheral site of human butyrylcholinesterase - Macdonald_2012_Biochemistry_51_7046
Author(s) : Macdonald IR , Martin E , Rosenberry TL , Darvesh S
Ref : Biochemistry , 51 :7046 , 2012
Abstract : Macdonald_2012_Biochemistry_51_7046
ESTHER : Macdonald_2012_Biochemistry_51_7046
PubMedSearch : Macdonald_2012_Biochemistry_51_7046
PubMedID: 22901043

Title : Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept) to cholinesterases - Saxena_2003_Eur.J.Biochem_270_4447
Author(s) : Saxena A , Fedorko JM , Vinayaka CR , Medhekar R , Radic Z , Taylor P , Lockridge O , Doctor BP
Ref : European Journal of Biochemistry , 270 :4447 , 2003
Abstract : Saxena_2003_Eur.J.Biochem_270_4447
ESTHER : Saxena_2003_Eur.J.Biochem_270_4447
PubMedSearch : Saxena_2003_Eur.J.Biochem_270_4447
PubMedID: 14622273

Title : Concentration-dependent reversible activation-inhibition of human butyrylcholinesterase by tetraethylammonium ion - Stojan_2002_Eur.J.Biochem_269_1154
Author(s) : Stojan J , Golicnik M , Froment MT , Estour F , Masson P
Ref : European Journal of Biochemistry , 269 :1154 , 2002
Abstract : Stojan_2002_Eur.J.Biochem_269_1154
ESTHER : Stojan_2002_Eur.J.Biochem_269_1154
PubMedSearch : Stojan_2002_Eur.J.Biochem_269_1154
PubMedID: 11856351

Title : Effects of mutations of active site residues and amino acids interacting with the Omega loop on substrate activation of butyrylcholinesterase - Masson_2001_Biochim.Biophys.Acta_1544_166
Author(s) : Masson P , Xie W , Froment MT , Lockridge O
Ref : Biochimica & Biophysica Acta , 1544 :166 , 2001
Abstract : Masson_2001_Biochim.Biophys.Acta_1544_166
ESTHER : Masson_2001_Biochim.Biophys.Acta_1544_166
PubMedSearch : Masson_2001_Biochim.Biophys.Acta_1544_166
PubMedID: 11341926
Gene_locus related to this paper: human-BCHE

Title : An improved cocaine hydrolase: the A328Y mutant of human butyrylcholinesterase is 4-fold more efficient - Xie_1999_Mol.Pharmacol_55_83
Author(s) : Xie W , Altamirano CV , Bartels CF , Speirs RJ , Cashman JR , Lockridge O
Ref : Molecular Pharmacology , 55 :83 , 1999
Abstract : Xie_1999_Mol.Pharmacol_55_83
ESTHER : Xie_1999_Mol.Pharmacol_55_83
PubMedSearch : Xie_1999_Mol.Pharmacol_55_83
PubMedID: 9882701

Title : Differences in active-site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase - Saxena_1999_Chem.Biol.Interact_119-120_61
Author(s) : Saxena A , Redman AM , Jiang X , Lockridge O , Doctor BP
Ref : Chemico-Biological Interactions , 119-120 :61 , 1999
Abstract : Saxena_1999_Chem.Biol.Interact_119-120_61
ESTHER : Saxena_1999_Chem.Biol.Interact_119-120_61
PubMedSearch : Saxena_1999_Chem.Biol.Interact_119-120_61
PubMedID: 10421439