Skip to main content
SpringerLink
Log in

Substrate Specificity of Cholinesterases in Various Representatives of the Animal Kingdom

  • Reviews
  • Published:
Journal of Evolutionary Biochemistry and Physiology Aims and scope Submit manuscript

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Stedmann, E., Stedmann, E., and Easson, L.H., Choline-esterase. An enzyme present in a blood–serum of the horse, Biochem. J., 1932, vol. 26, pp. 2056–2066.

    Article  Google Scholar 

  2. Vahlquist, B., On the esterase activity of human blood plasma, Skand. Arch. Physiol., 1935, vol. 72, pp. 133–160.

    Article  CAS  Google Scholar 

  3. Alles, G.A. and Hawes, R.C., Cholinesterases in the blood of man, J. Biol. Chem., 1940, vol. 133, pp. 375–390.

    CAS  Google Scholar 

  4. Mendel, B. and Rudney, H., Studies on cholinesterase. Cholinesterase and pseudo-cholinesterase, Biochem. J., 1943, vol. 37, pp. 59–63.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  5. Augustisson, K.-B., Studies of blood choline esterase, Ark. Kemi, Miner. Geol., 1944, vol. 18-A, no. 24, pp.1–16.

    Google Scholar 

  6. Augustisson, K.-B., Classification and comparative enzymology of the cholinesterases, and methods of their determination. In: cholinesterases and anticholinesterase agents, Handbuch der Experim. Pharmacologie, vol. 15, Koelle, G.B., Ed., Berlin, Goettingen, Heidelberg, 1963, pp. 89–129.

    Google Scholar 

  7. Aldridge, W.N., The differentiation of true and pseudo cholinesterase by organophosphorus compaunds, Biochem. J., 1953, vol. 53, pp. 63–67.

    Google Scholar 

  8. Golikov, S.N. and Rozengart, V.I., Farmakologiya i toksikologiya fosfororganicheskikh soedineniy (Pharmacology and Toxicology of Organophosphorous Compounds), Leningrad, 1960.

    Google Scholar 

  9. Golikov, S.N. and Rozengart, V.I., Kholinesterazy i antikholinesteraznye veshchestava (Cholinesterases and Anticholinesterase Substances), Leningrad, 1964.

    Google Scholar 

  10. Usdin, E., Reaction of cholinesterases with substrates, inhibitors and reactivators, Anticholinesterase Agents: Intern. Encycl. Pharmacol. Therap., Sect.13, Karczmar, A.G., Usdin, E., and Wills, J.H., Eds., Oxford, New York, 1970, vol. 1, pp. 47–356.

    Google Scholar 

  11. Brestkin, A.P., Brick, I.L.,and Grigor’eva, G.M., Comparative pharmacology of cholinesterases, Intern. Encycl. Pharmacol. Therap., sect. 85, Michelson, M.J., Ed., Oxford, New York, 1973, vol. 1, pp. 241–344.

    Google Scholar 

  12. Sadykov, A.S., Rozengart, E.V., Abduvakhabov, A.A., and Aslanov, Kh.A., Kholinesterazy. Aktivniy tsentr i mekhanizmy deistviya (Cholinesterases. Active Center and Mechanisms of Action), Tashkent, 1976.

    Google Scholar 

  13. Silver, A., The Biology of Cholinesterases, Amsterdam, 1974.

    Google Scholar 

  14. Brestkin, A.P., Kuznetsova, L.P., Moralev, S.N., Rozengart, E.V., and Epshtein, L.M., Kholinesterazy nazemnykh zhivotnykh i gidrobiontov (Cholinesterases of Terrestrial Animals and Hydrobionts), Vladivostok, 1997.

    Google Scholar 

  15. Moralev, S.N. and Rozengart, E.V., Comparative Enzymology of Cholinesterases, La Jolla, 2007.

    Google Scholar 

  16. Cousin, X., Bon, S., Duval, N., Massoulié, J., and Bon, C., Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. A new type of COOH-terminal domain; involvement of a positively charged residue in the peripheral site, J. Biol. Chem., 1996, vol. 271, pp. 15099–15108.

    Article  PubMed  CAS  Google Scholar 

  17. Brestkin, A.P., Zhukovsky, Yu.G., and Sipenkova, T.M., Hydrolysis of choline and thiocholine esters under the effect of cholinesterases, Biokhim., 1974, vol. 39, pp. 13–18.

    CAS  Google Scholar 

  18. Stojan, J., Marcel, V., Estrada-Mondaca, S., Klaebe, A., Masson, P., and Fournier, D., A putative kinetic model for substrate metabolisation by Drosophila acetylcholinesterase, FEBS Letters, 1998, vol. 440, pp. 85–88.

    Article  PubMed  CAS  Google Scholar 

  19. Marcel, V., Palacios, L.G., Pertuy, C., Masson, P., and Fournier, D., Two invertebrate acetylcholinesterase show activation followed by inhibition with substrate concentration, Biochem. J., 1998, vol. 329, pp. 329–334.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  20. Brestkin, A.P. and Pevzner, D.L., On the properties of acetylcholinesterase from the bovine brain and erythrocytes, Biokhim., 1971, vol. 36, pp. 81–86.

    CAS  Google Scholar 

  21. Brestkin, A.P. and Parkhomenko, T.V., Substrate specificity of partially purified cholinesterase from the chicken blood serum, Biokhim., 1971, vol. 36, pp. 950–955.

    CAS  Google Scholar 

  22. Brestkin, A.P., Zhukovsky, Yu.G., and Fartseiger, N.L., Catalytic properties of cholinesterases from the pigeon Columba livia brain and blood serum, Zh. Evol. Biokhim. Fiziol., 1983, vol. 19, pp. 138–143.

    CAS  Google Scholar 

  23. Brik, I.L. and Mandelstam, Yu.E., Properties of cholinesterases from the locust Locusta migratoria nervous system, Zh. Evol. Biokhim. Fiziol., 1973, vol. 9, pp. 138–143.

    PubMed  CAS  Google Scholar 

  24. Brick, I.L., Brestkin, A.P., and Mandelstam, Yu.E., Properties of cholinesterase and carboxylesterase of nervous tissue of Periplaneta Americana, Insect. Biochem., 1979, vol. 9, pp. 397–401.

    Article  Google Scholar 

  25. Voss, G. and Matsumure, F., Biochemical studies in a modified and normal cholinesterase found in the Leverkusen strains of the two-spotted spider mite Tetranychus urticae, Can. J. Biochem., 1965, vol. 43, pp. 63–72.

    Article  PubMed  CAS  Google Scholar 

  26. Myers, D.K., Studies on cholinesterase. 9. Species variations in the specificity pattern on the pseudocholinesterases, Biochem. J., 1953, vol. 55, pp. 67–79.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  27. Brestkin, A.P., Khovanskikh, A.E., Maizel, E.B., Moralev, S.N., Novozhilov, K.V., Sazonova, I.N., Abduvakhabov, A.A., Godovikov, N.N., Kabachnik, M.I., Khaskin, B.A., Mastryukova, T.A., and Shipov, A.E., Cholinesterases of aphids–II. Anticholinesterase potency and toxicity of different organophosphorous inhibitors for spring grain aphid Schizaphis gramina Rond, Insect. Biochem., 1986, vol. 16, pp. 701–707.

    Article  CAS  Google Scholar 

  28. Charyeva, O.B., Kulieva, A.M., Moralev, S.N., and Rozengart, V.I., Cholinesterases of the cotton bollworm (Heliothis armigera Hbn.), Izv. AN Turkmen. SSR, Ser. Biol. Nauk, 1991, no. 3, pp. 78–80.

    Google Scholar 

  29. Lockridge, O., Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine, Pharmacol. Ther., 1990, vol. 47, pp. 35–60.

    Article  PubMed  CAS  Google Scholar 

  30. Boeck, A.T., Schopfer, L.M., and Lockridge, O., DNA sequence of butyrylcholinesterase from the rat: expression of the protein and characterization of the properties of rat butyrylcholinesterase, Biochem. Pharmacol., 2002, vol. 63, pp. 2101–2110.

    Article  PubMed  CAS  Google Scholar 

  31. Reiner, E., Škrinjaric-Špoljar, M., Karlj, M., and Krvavica, S., Kinetic properties of the cholinesterase in Metastrongylus apri (Nematoda): substrate hydrolysis and reaction with organophosphorus compounds, Comp. Biochem. Physiol., 1978, vol. 60, pp. 155–157.

    CAS  Google Scholar 

  32. Augustinsson, K.B. and Nachmansohn, D., Distinction between acetylcholine-esterase and other choline ester-splitting enzymes, Science, 1949, vol. 110, pp. 98–99.

    Article  PubMed  CAS  Google Scholar 

  33. Brestkin, A.P., Rozengart, E.V., and Epshtein, L.M., On the properties of cholinesterase from the caudate nucleus of the seal Phoca hispida ladogensis brain, Zh. Evol. Biokhim. Fiziol., 1971, vol. 7, pp. 474–477.

    CAS  Google Scholar 

  34. Rozengart, E.V., Khovanskikh, A.E., Basova, N.E., and Moralev, S.N., Comparative enzymologic study of catalytic properties of brain cholinesterase of the mink Mustela vison, J. Evol. Bioch. Physiol., 2003, vol. 39, no.3, pp. 306–313.

    Article  CAS  Google Scholar 

  35. Rozengart, E.V., Khovanskikh, A.E., Basova, N.E., and Moralev, S.N., Comparative enzymologic study of catalytic properties of blood serum cholinesterase of the American mink Mustela vison, J. Evol. Bioch. Physiol., 2002, vol. 38, no. 4, pp. 401–406.

    Article  CAS  Google Scholar 

  36. Brik, I.L. and Yakovlev, V.A., Comparative investigation of properties of cholinesterases from the nervous system of vertebrates and insects, Biokhim., 1962, vol. 27, pp. 993–1003.

    CAS  Google Scholar 

  37. Metcalf, R.L. and March, R.B., Properties of acetylcholine esterases from the bee, the fly and the mouse and their relation to insecticide action, J. Econ. Entomol., 1950, vol. 43, pp. 670–677.

    Article  CAS  Google Scholar 

  38. Radic, Z. and Taylor, P., Interaction kinetics of reversible inhibitors and substrates with acetylcholinesterase and its fasciculin 2 complex, J. Biol. Chem., 2001, vol. 276, pp. 4622–4633.

    Article  PubMed  CAS  Google Scholar 

  39. Simon, S., Le Goff, A., Frobert, Y., Grassi, J., and Massoulie, J., The binding sites of inhibitory monoclonal antibodies on acetylcholinesterase. Identification of a novel regulatory site at the putative “back door”, J. Biol. Chem., 1999, vol. 274, pp. 27740–27746.

    Article  PubMed  CAS  Google Scholar 

  40. Morel, N. and Massoulie, J., Expression and processing of vertebrate acetylcholinesterase in the yeast Pichia pastoris, Biochem. J., 1997, vol. 328, pp. 121–129.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  41. Augustinsson, K.B., Substrate concentration and specificity of choline ester-splitting enzymes, Arch. Biochem., 1949, vol. 23, pp. 111–126.

    PubMed  CAS  Google Scholar 

  42. Frobert, Y., Creminon, C., Cousin, X., Remy, M.H., Chatel, J.M., Bon, S., Bon, C., and Grassi, J., Acetylcholinesterases from Elapidae snake venoms: biochemical, immunological and enzymatic characterization, Biochim. Biophys. Acta, 1997, vol. 1339, pp. 253–267.

    Article  PubMed  CAS  Google Scholar 

  43. Cunha Bastos, V.L.F., Rossini, A., Ribeiro Pinto, L.F., de Lima, L.M., Ceccarelli, P.S., Coelho, M.G.P., and Cunha Bastos, J., Different sensitivities to paraoxon of brain and serum cholinesterases from pacu, an indigenous Brazilian fish, Bull. Environ. Contam. Toxicol., 1998, vol. 60, pp.1–8.

    Article  CAS  Google Scholar 

  44. Moralev, S.N., Esaulova, A.V., Kurapov, A.A., Rozengart, E.V., and Khovanskikh, A.E., The study of cholinesterase activity of the liver of some fish of Caspian Sea, Dokl. RAN, 2003, vol. 392, pp. 549–551.

    Google Scholar 

  45. Simon, S. and Massoulie, J., Cloning and expression of acetylcholinesterase from Electrophorus. Splicing pattern of the 39 exons in vivo and in transfected mammalian cells, J. Biol. Chem., 1997, vol. 272, pp. 33045–33055.

    Article  PubMed  CAS  Google Scholar 

  46. Brestkin, A.P., Grigoryeva, G.M., Eremeeva, A.M., Zhukovsky, Yu.G., Kuznetsova, L.P., and Raki, L., Acetylcholinesterase in the electric organ of Torpedo marmorata, Zh. Evol. Biokhim. Fiziol., 1975, vol. 11, pp. 250–257.

    PubMed  CAS  Google Scholar 

  47. Pezzementi, L., Johnson, K., Tsigelny, I., Cotney, J., Manning, E., Barker, A., and Merritt, S., Amino acids defining the acyl pocket of an invertebrate cholinesterase, Comp. Biochem. Physiol., 2003, vol. 136B, pp. 813–832.

    Article  CAS  Google Scholar 

  48. Roan, C.C. and Maeda, S., The cholinesterase of the oriental fruit fly and its in vitro reactions with various insecticides compounds, J. Econ. Entomol., 1953, vol. 46, pp. 755–779.

    Article  Google Scholar 

  49. Grigoryeva, G.M., Krasnova, T.I., Khovanskikh, A.E., Gusev, G.V., and Lezhneva, I.P., Isolation and catalytic properties of soluble and membrane-bound cholinesterases from the fly Delia brassicae brain, Biokhim., 1987, vol. 52, pp.1192–1200.

    Google Scholar 

  50. Grigoryeva, G.M., Krasnova, T.I., Khovanskikh, A.E., and Lezhneva, I.P., Substrate and inhibitor specificity of cholinesterase in the brain of different dipteran species (Diptera: Anthomiidae, Muscidae), Zh. Evol. Biokhim. Fiziol., 1997, vol. 33, pp. 431–438.

    Google Scholar 

  51. Kunkee, R.E. and Zweig, G., Substrate specificity studies on bee acetylcholinesterase purified by gradient centrifugation, J. Insect. Physiol., 1963, vol. 9, pp. 495–507.

    Article  CAS  Google Scholar 

  52. Guilbaut, G.G., Huan, S.S., and Sadar, M.H., Purification and properties of cholinesterases from honey bee Apis mellifera Linnaeus and boll weeviels Anthonomus grandis Boheman, J. Agric. Food. Chem., 1970, vol. 18, p.692.

    Article  Google Scholar 

  53. Sazonova, I.N., Nikanorova, E.V., and Shvets, E.K., Action selectivity of hostaquick and pirimor in aphids and their entomophages, Problemy izbiratelnosti deistviya insektitsidov i akaritsidov i ee znachenie v zashchite rastenii (The Problem of Action Selectivity of Insecticides and Acaricides and its Significance for Plant Protection), Leningrad, 1986, pp. 48–59.

    Google Scholar 

  54. Guedes, R.N.C., Zhu, K.Y., Kambhampati, S., and Dover, B.A., An altered acetylcholinesterase conferring negative cross-insensitivity to different insecticidal inhibitors in organophosphate-resistant lesser grain borer, Rhyzopertha dominica, Pestic. Biochem. Physiol., 1997, vol. 58, pp. 55–62.

    Article  CAS  Google Scholar 

  55. Charyeva, O.B., Substrate–inhibitor characterization of cholinesterases in the cotton bollworm Heliothis armigera Hbn., Candidate Diss., Ashkhabad, 1995.

    Google Scholar 

  56. Wood, E., Zerba, E., Picollo, M., and de Licastro, S., Partial purification and characterization of Triatoma infestans head cholinesterase, Insect. Biochem., 1979, vol. 9, pp. 595–601.

    Article  CAS  Google Scholar 

  57. Hama, H., Iwata, T., Miyata, T., and Saito, T., Some properties of acetylcholinesterase partially purified from susceptible and resistant green rice leafhoppres, Nephotettix cincticeps Uhler (Hemiptera: Deltocephalidae), Appl. Entomol. Zool., 1980, vol. 15, pp. 249–261.

    Article  CAS  Google Scholar 

  58. Yerushalmi, N. and Cohen, E., Acetylcholinesterase of the California red scale Aonidiella aurantii Mask.: catalysis, inhibition, and reactivation, Pestic. Biochem. Physiol., 2002, vol. 72, pp. 133–141.

    Article  CAS  Google Scholar 

  59. Gao, J.R. and Zhu, K.Y., An acetylcholinesterase purified from the greenbug (Schizaphis graminum) with some unique enzymological and pharmacological characteristics, Insect. Biochem. Mol. Biol., 2001, vol. 31, pp. 1095–1104.

    Article  PubMed  CAS  Google Scholar 

  60. Tilyabaev, Z., Properties of cholinesterase and carboxylesterase in nervous tissue of the locust Locusta migratoria, Zh. Evol. Biokhim. Fiziol., 1978, vol. 14, pp. 405–407.

    CAS  Google Scholar 

  61. Lee, A.-H., Metcalf, R.L., and Kearns, C.W., Purification and some properties of house cricket (Acheta domesticus) acetylcholinesterase, Insect. Biochem., 1974, vol. 4, pp. 267–280.

    Article  CAS  Google Scholar 

  62. Brick, I.L., Brestkin, A.P., Mandelstam, Yu.E., and Sazonova, I.N., Substrate and inhibitor specificity of cholinesterases from certain insects, Environmental Quality and Safety, Suppl. Vol. III., Coulston, F. and Korte, F., Ed., Lectures held at the IUPAC Third Int. Congr. Pest. Chem., Helsinki, July 3–9, 1974, Stuttgart, 1975, pp. 539–543.

    Google Scholar 

  63. Brestkin, A.P., Vinyar, T.N., and Rozengart, E.V., Interaction of cholinesterase from Pacific squid visual ganglion with some ammonium compounds, Neirokhim., 1982, vol. 1, pp. 28–35.

    Google Scholar 

  64. Grigoryeva, G.M., Cholinesterase of visual ganglion in the octopus Octopus sp. And the squid Ommastrephes sloanei pacificus, Fermenty v evolyutsii zhivotnykh (Enzymes in Evolution of Animals), Leningrad, 1969, pp. 177–183.

    Google Scholar 

  65. Shevtsova, S.P., Brestkin, A.P., Nesis, K.N., and Rozengart, E.V., On the identity of properties of cholinesterases in optic ganglion of the squid Ommatostrephes bartrami from the South Atlantic and the Great Australian Bight, Okeanol., 1977, vol. 17, pp. 1102–1105.

    CAS  Google Scholar 

  66. Grigoryeva, G.M., Cholinesterase of visual ganglion in the squid Illex illecebrosus, cuttlefish Sepia officinalis and eledone Eledone sp., Sravnitel’naya neirofiziologiya i neirokhimiya (Comparative Neurophysiology and Neurochemistry), Kreps, E.M., Ed., Leningrad, 1976, pp. 3–13.

    Google Scholar 

  67. Talesa, V., Grauso, M., Arpagaus, M., and Giovannini, E., Romani, R., and Rosi, G., Molecular cloning and expression of a full-length cDNA encoding acetylcholinesterase in optic lobes of the squid Loligo opalescens: a new member of the cholinesterase family resistant to diisopropyl fluorophosphates, J. Neurochem., 1999, vol. 72, pp. 1250–1258.

    Article  PubMed  CAS  Google Scholar 

  68. Grigoryeva, G.M., Propionyl cholinesterase in the brain of gastropod mollusks. Interaction with substrates and inhibitors, Biokhim., 1980, vol. 45, pp. 2176–2188.

    Google Scholar 

  69. Grigoryeva, G.M. and Tkachenko, S.S., Cholinesterase in the hemolymph of gastropod mollusks, Zh. Evol. Biokhim. Fiziol., 1971, vol. 7, pp. 254–261.

    Google Scholar 

  70. Grigoryeva, G.M., Comparative investigation of cholinesterases in nerve tissue of cephalopod and gastropod mollusks, Sravnitelnaya farmakologiya sinapticheskikh retseptorov (Comparative Pharmacology of Synaptic Photoreceptors), Kreps, E.M., Ed., Leningrad, 1977, pp. 137–143.

    Google Scholar 

  71. Grigoryeva, G.M., Catalytic properties and sensitivity to different inhibitors of cholinesterase from salivary glands of the mollusk Murex trunculus (Gastropoda), Biokhim., 1973, vol. 38, pp.1126–1135.

    Google Scholar 

  72. Bocquene, G., Roig, A., and Fournier, D., Cholinesterases from the common oyster (Crassostrea gigas). Evidence for the presence of a soluble acetylcholinesterase insensitive to organophosphate and carbamate inhibitors, FEBS Lett., 1997, vol. 407, pp. 261–266.

    Article  PubMed  CAS  Google Scholar 

  73. Knowles, C.O. and Casida, J.E., Mode of action of organophosphate antihelmintics: cholinesterase inhibition in Ascaris lumbricoides, J. Agric. Food. Chem., 1966, vol. 14, pp. 566–572.

    Article  CAS  Google Scholar 

  74. Hussein, A.S., Chacon, M.R., Smith, A.M., Tosado-Acevedo, R., and Selkirk, M.E., Cloning, expression, and properties of a nonneuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis, J. Biol. Chem., 1999, vol. 274, pp. 9312–9319.

    Article  PubMed  CAS  Google Scholar 

  75. Reiner, E., Esterases in Schistosomes: reaction with substrates and inhibitors, Acta Pharm. Toxicol., 1981, vol. 49, pp. 72–78.

    Article  CAS  Google Scholar 

  76. Hosea, N.A, Berman, H.A, and Taylor, P., Specificity and orientation of trigonal carboxyl esters and tetrahedral alkylphosphonyl esters in cholinesterases, Biochemistry, 1995, vol. 34, pp. 11528–11536.

    Article  PubMed  CAS  Google Scholar 

  77. Abramovitch, T.D., Borzunina, A.M., Golub, T.L., Eremeeva, A.M., Zhukovsky, Yu.G., Kuznetsova, L.P., Maksimova, G.I., Pushkarev, V.V., Sochilina, E.E., and Epshtein, L.M., On the catalytic properties of cholinesterase from human erythrocytes, Biokhim., 1973, vol. 38, pp. 1137–1143.

    Google Scholar 

  78. Metcalf, R.L., March, R.B., and Maxon, M.G., Substrate preferences of insect cholinesterases, Ann. Entom. Soc. Amer., 1955, vol. 48, pp. 222–228.

    Article  CAS  Google Scholar 

  79. Basova, N.E., Kormilitsyn, B. I., Rozengart, E.V., Saakov, V. S., and Suvorov, A. A., Comparative sensitivity of cholinesterases in vertebrates and invertebrates to highly specific organophosphorus inhibitors, diisopropyl fluorophosphate (DFP) and (2-ethoxymethyl phosphoryl thioethyl) ethyl (methyl) sulphonium sulphomethylate (GD-42), J. Evol. Biochem. Physiol., 2015, vol. 51, no. 6, pp. 471–479.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, St. Petersburg, Russia

    N. E. Basova, B. N. Kormilitsyn, A. Yu. Perchenok, E. V. Rozengart, V. S. Saakov & A. A. Suvorov

Authors
  1. N. E. Basova
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. B. N. Kormilitsyn
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. A. Yu. Perchenok
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. E. V. Rozengart
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. V. S. Saakov
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. A. A. Suvorov
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to N. E. Basova.

Additional information

Original Russian Text © N.E. Basova, B.N. Kormilitsyn, A.Yu. Perchenok, E.V. Rozengart, V.S. Saakov, A.A. Suvorov, 2018, published in Zhurnal Evolyutsionnoi Biokhimii i Fiziologii, 2018, Vol. 54, No. 3, pp. 141–153.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Basova, N.E., Kormilitsyn, B.N., Perchenok, A.Y. et al. Substrate Specificity of Cholinesterases in Various Representatives of the Animal Kingdom. J Evol Biochem Phys 54, 157–174 (2018). https://doi.org/10.1134/S0022093018030018

Download citation

  • Received:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1134/S0022093018030018

Key words

Search

Navigation