E450A_human-ACHE

General

Gene Locus : human-ACHE

Mode of mutation : Site directed mutagenesis

Disease :

Summary : Catalysis Catalysis\/H-bond network\/active center modulation, reduced kapp for ACT and TB Ordentlich_1993_FEBS.Lett_334_215 Ordentlich_1995_5th.ChE.Meeting.Madras__221 Shafferman_1995_5th.ChE.Meeting.Madras__189 || Heat and pressure stability strengthened heat stability decreased pressure stability Clery-Barraud_2002_Eur.J.Biochem_269_4297

AAA Change :

Allelic Variant :

Risk Factor :

Inhibitor :

Structure :

Disease by interaction :

Interact Gene Locus :

Xenobiotic sensitivity :

Modification : H-bond network || Catalysis || Heat and pressure stability || Stability

Torpedo_number : 443

Kinetic Parameter : Tacrine_E450A_human-ACHE, HuperzineA_E450A_human-ACHE

News : No news

Comment :
p.E450A Glu450Ala (p.E481A Glu481Ala in primary sequence with 31 amino-acids signal peptide) Catalysis\/H-bond network\/active center modulation, reduced kapp for ACT and TB\; Heat and pressure stability: strengthened heat stability decreased pressure stability

References (5)

Title : Pressure and heat inactivation of recombinant human acetylcholinesterase. Importance of residue E202 for enzyme stability - Clery-Barraud_2002_Eur.J.Biochem_269_4297
Author(s) : Clery-Barraud C , Ordentlich A , Grosfeld H , Shafferman A , Masson P
Ref : European Journal of Biochemistry , 269 :4297 , 2002
Abstract : Clery-Barraud_2002_Eur.J.Biochem_269_4297
ESTHER : Clery-Barraud_2002_Eur.J.Biochem_269_4297
PubMedSearch : Clery-Barraud_2002_Eur.J.Biochem_269_4297
PubMedID: 12199708

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 : Amino Acids Determining Specificity to OP-Agents and Facilitating the Aging Process in Human Acetylcholinesterase -
Author(s) : Ordentlich A , Kronman C , Stein D , Ariel N , Reuveny S , Marcus D , Segall Y , Barak D , Velan B , Shafferman A
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. :221 , 1995
PubMedID:

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 : Engineering resistance to 'aging' of phosphylated human acetylcholinesterase. Role of hydrogen bond network in the active center - Ordentlich_1993_FEBS.Lett_334_215
Author(s) : Ordentlich A , Kronman C , Barak D , Stein D , Ariel N , Marcus D , Velan B , Shafferman A
Ref : FEBS Letters , 334 :215 , 1993
Abstract : Ordentlich_1993_FEBS.Lett_334_215
ESTHER : Ordentlich_1993_FEBS.Lett_334_215
PubMedSearch : Ordentlich_1993_FEBS.Lett_334_215
PubMedID: 8224249