Gene Locus : human-BCHE
Mode of mutation : Site directed mutagenesis
Disease :
Summary : Subunit assembly Elimination of interchain disulfide bond, decreases heat stability but preserves tetrameric structure Blong_1995_5th.ChE.Meeting.Madras__129 Blong_1997_Biochem.J_327_747
AAA Change :
Allelic Variant :
Risk Factor :
Inhibitor :
Structure :
Disease by interaction :
Interact Gene Locus :
Xenobiotic sensitivity :
Modification : Subunit assembly || Stability
Torpedo_number : 572
Kinetic Parameter : No kinetic parameter
News : No news
Comment :
p.C571A Cys571Ala (p.C601A Cys601Ala in primary sequence with 28 amino-acids signal peptide) Elimination of interchain disulfide bond, decreases heat stability but preserves tetrameric structure
Title : Association of tetramers of human butyrylcholinesterase is mediated by conserved aromatic residues of the carboxy terminus - Altamirano_1999_Chem.Biol.Interact_119-120_53 |
Author(s) : Altamirano CV , Lockridge O |
Ref : Chemico-Biological Interactions , 119-120 :53 , 1999 |
Abstract : |
PubMedSearch : Altamirano_1999_Chem.Biol.Interact_119-120_53 |
PubMedID: 10421438 |
Title : Conserved aromatic residues of the C-terminus of human butyrylcholinesterase mediate the association of tetramers - Altamirano_1999_Biochemistry_38_13414 |
Author(s) : Altamirano CV , Lockridge O |
Ref : Biochemistry , 38 :13414 , 1999 |
Abstract : |
PubMedSearch : Altamirano_1999_Biochemistry_38_13414 |
PubMedID: 10529218 |
Title : Tetramerization domain of human butyrylcholinesterase is at the C- terminus - Blong_1997_Biochem.J_327_747 |
Author(s) : Blong RM , Bedows E , Lockridge O |
Ref : Biochemical Journal , 327 :747 , 1997 |
Abstract : |
PubMedSearch : Blong_1997_Biochem.J_327_747 |
PubMedID: 9581552 |
Title : Subunit Association and Stabilization of Butyrylcholinesterase (BChE) - |
Author(s) : Blong RM , Masson P , Lockridge O |
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. :129 , 1995 |
PubMedID: |