Sensitivity of Cholinesterases of Different Origin to Organophosphorus Inhibitors with S-Alkyl Radical of Different Length
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- Kormilitsyn, B.N., Moralev, S.N., Khovanskikh, A.E. et al. Journal of Evolutionary Biochemistry and Physiology (2003) 39: 505. doi:10.1023/B:JOEY.0000015957.68399.21
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An antienzyme potency of 18 organophosphorus inhibitors (OPI), S-alkyl derivatives of thiophosphoric and thiophosphonic acids, to acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) of the spring grain aphid and corresponding mammalian enzymes is studied. It is shown that dependence of the inhibitory potency on length of alkyl radicals differs in human and aphid AChE. Smaller differences were observed in the case of aphid and horse BuChE. The obtained data are compared to the data obtained at studying other series of OPI and cholinesterases of other animals. It is suggested that the revealed peculiarity of the inhibitory specificity of aphid AChE is due to the presence of serine instead of phenylalanine in the position 331 (the numeration according to AChE of the electric ray Torpedo californica).