Substrate Specificity of Cholinesterases in Various Representatives of the Animal Kingdom


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Abstract

This review summarizes the literature data as well as experimental results obtained at our Institute over a period of 50 years on the substrate specificity of cholinesterases–acetylcholine acetylhydrolases (EC 3.1.1.7) and acylcholine acylhydrolases (EC 3.1.1.8). The parameters of enzymatic hydrolysis of oxo- and thiocholine and β-methylcholine esters in different organs and tissues were analyzed in 66 animal species including 22 chordate, 20 insect, 1 mite, 17 mollusk, 4 nematode, and 2 flatworm species. Our substrate specificity studies and extensive data on the inhibitory specificity obtained using irreversible organophosphorous inhibitors and reversible effectors unequivocally indicate that the cholinesterase family is characterized by a clear-cut species and tissue specificity.

About the authors

N. E. Basova

Sechenov Institute of Evolutionary Physiology and Biochemistry

Author for correspondence.
Email: roz@iephb.ru
Russian Federation, St. Petersburg

B. N. Kormilitsyn

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: roz@iephb.ru
Russian Federation, St. Petersburg

A. Yu. Perchenok

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: roz@iephb.ru
Russian Federation, St. Petersburg

E. V. Rozengart

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: roz@iephb.ru
Russian Federation, St. Petersburg

V. S. Saakov

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: roz@iephb.ru
Russian Federation, St. Petersburg

A. A. Suvorov

Sechenov Institute of Evolutionary Physiology and Biochemistry

Email: roz@iephb.ru
Russian Federation, St. Petersburg

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