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https://doi.org/10.5562/cca1815

Reactivation of Tabun-inhibited Acetylcholinesterase Investigated by Two Oximes and Mutagenesis

Maja Katalinić   ORCID icon orcid.org/0000-0001-7043-4291 ; Institute for Medical Research and Occupational Health, P.P. 291, HR-10001 Zagreb, Croatia
Zrinka Kovarik   ORCID icon orcid.org/0000-0001-9863-886X ; Institute for Medical Research and Occupational Health, P.P. 291, HR-10001 Zagreb, Croatia

Puni tekst: engleski, pdf (2 MB) str. 209-212 preuzimanja: 760* citiraj
APA 6th Edition
Katalinić, M. i Kovarik, Z. (2012). Reactivation of Tabun-inhibited Acetylcholinesterase Investigated by Two Oximes and Mutagenesis. Croatica Chemica Acta, 85 (2), 209-212. https://doi.org/10.5562/cca1815
MLA 8th Edition
Katalinić, Maja i Zrinka Kovarik. "Reactivation of Tabun-inhibited Acetylcholinesterase Investigated by Two Oximes and Mutagenesis." Croatica Chemica Acta, vol. 85, br. 2, 2012, str. 209-212. https://doi.org/10.5562/cca1815. Citirano 08.03.2021.
Chicago 17th Edition
Katalinić, Maja i Zrinka Kovarik. "Reactivation of Tabun-inhibited Acetylcholinesterase Investigated by Two Oximes and Mutagenesis." Croatica Chemica Acta 85, br. 2 (2012): 209-212. https://doi.org/10.5562/cca1815
Harvard
Katalinić, M., i Kovarik, Z. (2012). 'Reactivation of Tabun-inhibited Acetylcholinesterase Investigated by Two Oximes and Mutagenesis', Croatica Chemica Acta, 85(2), str. 209-212. https://doi.org/10.5562/cca1815
Vancouver
Katalinić M, Kovarik Z. Reactivation of Tabun-inhibited Acetylcholinesterase Investigated by Two Oximes and Mutagenesis. Croatica Chemica Acta [Internet]. 2012 [pristupljeno 08.03.2021.];85(2):209-212. https://doi.org/10.5562/cca1815
IEEE
M. Katalinić i Z. Kovarik, "Reactivation of Tabun-inhibited Acetylcholinesterase Investigated by Two Oximes and Mutagenesis", Croatica Chemica Acta, vol.85, br. 2, str. 209-212, 2012. [Online]. https://doi.org/10.5562/cca1815

Sažetak
The reactivation of tabun-inhibited AChE site-directed mutants assisted by two bispyridinium oximes, K048 (N-[4-(4-hydroxyiminomethylpyridinio)butyl]-4-carbamoylpyridinium dibromide) and K033 ((N,N' -butano)bis(2-hydroxyiminomethylpyridinium bromide) was studied to analyse the constraints on oxime-assisted reactivation. AChE was modified within the acyl (F295L, F297I) and choline (Y337A) binding site of the active site gorge. Results show that introduced mutations affected both the affinity of phosphorylated enzyme for oximes and the rate of nucleophilic displacement of phosphoryl moiety from the catalytic serine. Mutations significantly lowered the overall reactivation efficacy of K048, but slightly enhanced the potency of K033 to reactivate tabun-inhibited AChE. It seems that the replacement of aromatic residues with the aliphatic ones at the acyl and choline binding site greatly interfered with the stabilization of the oxime's pyridinium ring(s) within the active site gorge needed to obtain the proper orientation of the oxime group toward the phosphorylated active site serine. (doi: 10.5562/cca1815)

Ključne riječi
acetylcholinesterase; butyrylcholinesterase; nerve agents; oxime; protection; reactivation

Hrčak ID: 81254

URI
https://hrcak.srce.hr/81254

Posjeta: 1.124 *