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Acetylcholinesterase mutants: oxime-assisted catalytic scavengers of organophosphonates (CROSBI ID 739874)

Prilog sa skupa u časopisu | izvorni znanstveni rad

Kovarik, Zrinka ; Radić, Zoran ; Simeon-Rudolf, Vera ; Reiner, Elsa ; Taylor, Palmer Acetylcholinesterase mutants: oxime-assisted catalytic scavengers of organophosphonates // Chemico-biological interactions. 2005. str. 388-390-x

Podaci o odgovornosti

Kovarik, Zrinka ; Radić, Zoran ; Simeon-Rudolf, Vera ; Reiner, Elsa ; Taylor, Palmer

engleski

Acetylcholinesterase mutants: oxime-assisted catalytic scavengers of organophosphonates

instead abstract, part of the Introduction: Reaction of organophosphonates with acetylcholinesterase (AChE ; EC 3.1.1.7) is characterized by the formation of serine-conjugated adducts that are only slowly reversible. Since oximes are the only known antidote to nerve agent poisoning that restore the activity of AChE, mutagenesis of AChE should enable one to develop more effective scavenging agents in which AChE mutants in combination with an oxime would complete a catalytic cycle of hydrolysis of the organophosphate by rapid inhibition followed by rapid nucleophile-mediated hydrolysis of the phosphonyl enzyme conjugate. We enlarged the active site gorge of mouse AChE with mutations Y337A, F295L and F297I. Based on rapid inhibition of mutants with SP-cycloheptyl methylphosphonyl thiocholine (SP-CHMPTCh) and enhancement of their HI-6 reactivation rates up to 130-fold as compared to the AChE wild-type, we studied the continuous enzymatic decomposition of the SP-CHMPTCh by AChE mutants in the presence of HI-6.

acetylcholinesterase; reactivation; inhibition; organophosphorus compounds; oxime

Rad je pprošireni sažetak (Extended abstract)

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Podaci o prilogu

388-390-x.

2005.

nije evidentirano

objavljeno

Podaci o matičnoj publikaciji

Chemico-biological interactions

0009-2797

Podaci o skupu

Nepoznat skup

ostalo

29.02.1904-29.02.2096

Povezanost rada

Kemija

Indeksiranost