Kovarik_2006_Biochem.Biophys.Res.Commun_342_973

Reference

Title : Active site mutant acetylcholinesterase interactions with 2-PAM, HI-6, and DDVP - Kovarik_2006_Biochem.Biophys.Res.Commun_342_973
Author(s) : Kovarik Z , Ciban N , Radic Z , Simeon-Rudolf V , Taylor P
Ref : Biochemical & Biophysical Research Communications , 342 :973 , 2006
Abstract : We used mouse recombinant wild-type acetylcholinesterase (AChE; EC 3.1.1.7), butyrylcholinesterase (BChE; EC 3.1.1.8), and AChE mutants with mutations (Y337A, F295L, F297I, Y72N, Y124Q, and W286A) that resemble residues found at structurally equivalent positions in BChE, to find the basis for divergence between AChE and BChE in following reactions: reversible inhibition by two oximes, progressive inhibition by the organophosphorus compound DDVP, and oxime-assisted reactivation of the phosphorylated enzymes. The inhibition enzyme-oxime dissociation constants of AChE w.t. were 150 and 46 microM, of BChE 340 and 27 microM for 2-PAM and HI-6, respectively. Introduced mutations lowered oxime binding affinities for both oximes. DDVP progressively inhibited cholinesterases yielding symmetrical dimethylphosphorylated enzyme conjugates at rates between 104 and 105/min/M. A high extent of oxime-assisted reactivation of all conjugates was achieved, but rates by both oximes were up to 10 times slower for phosphorylated mutants than for AChE w.t.
ESTHER : Kovarik_2006_Biochem.Biophys.Res.Commun_342_973
PubMedSearch : Kovarik_2006_Biochem.Biophys.Res.Commun_342_973
PubMedID: 16598855

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Citations formats

Kovarik Z, Ciban N, Radic Z, Simeon-Rudolf V, Taylor P (2006)
Active site mutant acetylcholinesterase interactions with 2-PAM, HI-6, and DDVP
Biochemical & Biophysical Research Communications 342 :973

Kovarik Z, Ciban N, Radic Z, Simeon-Rudolf V, Taylor P (2006)
Biochemical & Biophysical Research Communications 342 :973