Gene Locus : human-BCHE
Mode of mutation : Site directed mutagenesis
Disease :
Summary : Search for phosphotriesterase activity Phosphotriesterase activity Identical to WT Lockridge_1997_Biochemistry_36_786 || Search for phosphotriesterase activity Phosphotriesterase activity OP sensitive Schopfer_2004_J.Med.Chem.Biol.Radiol.Def_2_1
AAA Change :
Allelic Variant :
Risk Factor :
Inhibitor :
Structure :
Disease by interaction :
Interact Gene Locus :
Xenobiotic sensitivity :
Modification : Search for phosphotriesterase activity
Torpedo_number : 288
Kinetic Parameter : No kinetic parameter
News : No news
Comment :
p.L286H Leu286His (p.L314H Leu314His in primary sequence with 28 amino-acids signal peptide) Phosphotriesterase activity Identical to WT. Tentative to place an Histidine in the active site at other place than the G117H mutation. Though the L286H mutant reactivated 400-fold more slowly than G117H, it was still 250-fold faster than wild-type BChE. Adjusting the position of histidine 286 by adding glycine residues to the sequence, e.g., L286GH, L286HG, and L286GHG, did not improve the reactivation rate
| Title : Mutants of human butyrylcholinesterase with organophosphate hydrolase activity\; evidence that His117 is a general base catalyst for hydrolysis of echothiophate - Schopfer_2004_J.Med.Chem.Biol.Radiol.Def_2_1 |
| Author(s) : Schopfer LM , Boeck AT , Broomfield CA , Lockridge O |
| Ref : Journal of Medicinal Chemistryical Biology Radiol Def , 2 :1 , 2004 |
| Abstract : |
| PubMedSearch : Schopfer_2004_J.Med.Chem.Biol.Radiol.Def_2_1 |
| PubMedID: |
| Title : A single amino acid substitution, Gly117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase - Lockridge_1997_Biochemistry_36_786 |
| Author(s) : Lockridge O , Blong RM , Masson P , Froment MT , Millard CB , Broomfield CA |
| Ref : Biochemistry , 36 :786 , 1997 |
| Abstract : |
| PubMedSearch : Lockridge_1997_Biochemistry_36_786 |
| PubMedID: 9020776 |