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Izvorni znanstveni članak
https://doi.org/10.5562/cca1815
Reactivation of Tabun-inhibited Acetylcholinesterase Investigated by Two Oximes and Mutagenesis
Maja Katalinić
orcid.org/0000-0001-7043-4291
; Institute for Medical Research and Occupational Health, P.P. 291, HR-10001 Zagreb, Croatia
Zrinka Kovarik
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 | citiraj | |
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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 |
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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
Moj profil
Srce