A328F_human-BCHE

General

Gene Locus : human-BCHE

Mode of mutation : Site directed mutagenesis

Disease :

Summary : 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 10-fold increase Ki vs WT Saxena_2003_Eur.J.Biochem_270_4447 || Cationic triarylmethane dyes Biberoglu_2011_Arch.Biochem.Biophys_511_64

AAA Change :

Allelic Variant :

Risk Factor :

Inhibitor :

Structure :

Disease by interaction :

Interact Gene Locus :

Xenobiotic sensitivity :

Modification : Acyl specificity || Substrate activation || Aricept~Donepezil~E2020 inhibition || Cationic triarylmethane dyes

Torpedo_number : 330

Kinetic Parameter : No kinetic parameter

News : No news

Comment : p.A328F Ala328Phe (p.A356F Ala356Phe in primary sequence with 28 amino-acids signal peptide) Substrate activation\; Aricept~Donepezil~E2020 inhibition\;10-fold increase Ki vs WT

References (4)

Title : The role of Phe329 in binding of cationic triarylmethane dyes to human butyrylcholinesterase - Biberoglu_2011_Arch.Biochem.Biophys_511_64
Author(s) : Biberoglu K , Tacal O , Akbulut H
Ref : Archives of Biochemistry & Biophysics , 511 :64 , 2011
Abstract : Biberoglu_2011_Arch.Biochem.Biophys_511_64
ESTHER : Biberoglu_2011_Arch.Biochem.Biophys_511_64
PubMedSearch : Biberoglu_2011_Arch.Biochem.Biophys_511_64
PubMedID: 21530486

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 : 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 : 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