Comprehensive Physiology Wiley Online Library

Hydrolytic Transformation of Environmental Pollutants

Full Article on Wiley Online Library


The sections in this article are:

1 Ester Hydrolysis
2 Organophosphorus Triesters
2.1 Phosphorylphosphatases (Fluorophosphatases)
2.2 Arylesterases
2.3 Carboxylesterases
2.4 Carboxyamidase
2.5 Other Hydrolytic Mechanisms
3 Carbamic Acid Esters
4 Pyrethyroid Ester Insecticides
5 Herbicide Esters
6 Phthalic Acid Esters
 1. Abernathy, C. O., and J. E. Casida. Pyrethroid insecticides. Esterase cleavage in relation to selective toxicity. Science 179: 1235–1236, 1973.
 2. Abernathy, C. O., K. Ueda, J. L. Engel, L. C. Gaughan, and J. E. Casida. Substrate‐specificity and toxicological significance of pyrethroid‐hydrolyzing esterases of mouse liver microsomes. Pesticide Biochem. Physiol. 3: 300–311, 1973.
 3. Adie, P. A., and J. Tuba. The intracellular localization of liver and kidney sarinase. Can. J. Biochem. Physiol. 36: 21–24, 1958.
 4. Albro, P. W., and R. O. Thomas. Enzymatic hydrolysis of di‐(2‐ethylhexyl) phthalate by lipases. Biochim. Biophys. Acta 360: 380–390, 1973.
 5. Albro, P. W., R. Thomas, and L. Fishbein. Metabolism of diethylhexyl phthalate by rats. Isolation and characterization of the urinary metabolites. J. Chromatog. 76: 321–330, 1973.
 6. Aldridge, W. N. Serum esterases. 1. Two types of esterase (A and B) hydrolyzing p‐nitrophenyl acetate, propionate and butyrate and a method for their determination. Biochem. J. 53: 110–117, 1953.
 7. Aldridge, W. N. Serum esterases. 2. An enzyme hydrolyzing diethyl p‐nitrophenyl phosphate (E 600) and its identity with the A‐esterase of mammalian serum. Biochem. J. 53: 117–124, 1953.
 8. Aldridge, W. N. The nature of the reaction of organophosphorus compounds and carbamates with esterases. Bull. World Health Organ. 44: 25–30, 1971.
 9. Aldridge, W. N., and E. Reiner. Enzyme Substrates as Inhibitors. Interaction of Esterases With Esters of Organophosphorus and Carbamic Acids. New York: Am. Elsevier, 1972.
 10. Augustsyn, R. C., J. De Jersey, E. C. Webb, and B. Zerher. On the homology of the active‐site peptides of liver carboxylesterases. Biochim. Biophys. Acta 171: 128–137, 1969.
 11. Augustinsson, K.‐B. The enzymic hydrolysis of organophosphorus compounds. Biochim. Biophys. Acta 13: 303–304, 1954.
 12. Augustinsson, K.‐B. Electrophoresis studies on blood plasma esterases. I. Mammalian plasmata. Acta Chem. Scand. 13: 571–592, 1959.
 13. Augustinsson, K.‐B. Electrophoresis studies on blood plasma esterases. II. Avian, reptilian, amphibian and piscine plasmata. Acta Chem. Scand. 13: 1081–1096, 1959.
 14. Augustinsson, K.‐B. Electrophoresis studies on blood plasma esterases. III. Conclusions. Acta Chem. Scand. 13: 1097–1105, 1959.
 15. Augustinsson, K.‐B. Multiple forms of esterase in vertebrate blood plasma. Ann. NY Acad. Sci. 94: 844–860, 1961.
 16. Augustinsson, K.‐B. Arylesterases. J. Histochem. Cytochem. 12: 744–747, 1964.
 17. Augustinsson, K.‐B., and J. E. Casida. Enzymic hydrolysis of N: N‐dimethylcarbamoyl fluoride. Biochem. Pharmacol. 3: 60–67, 1959.
 18. Augustinsson, K.‐B., and G. Ekedahl. On the specificity of arylesterases. Acta Chem. Scand. 16: 240–241, 1962.
 19. Augustinsson, K.‐B., and G. Heimburger. Enzymatic hydrolysis of organophosphorus compounds. I. Occurrence of enzymes hydrolyzing dimethyl‐amido‐ethoxy‐phosphoryl cyanide (Tabun). Acta Chem. Scand. 8: 753–761, 1954.
 20. Augustinsson, K.‐B., and G. Heimburger. Enzymatic hydrolysis of organophosphorus compounds. IV. Specificity studies. Acta Chem. Scand. 8: 1533–1541, 1954.
 21. Augustinsson, K.‐B., and G. Heimburger. Enzymatic hydrolysis of organophosphorus compounds. VI. Effects of metal ions on the phosphorylphosphatases of human serum and swine kidney. Acta Chem. Scand. 9: 383–392, 1955.
 22. Baron, R. L., J. L. Casterline, and O. G. Fitzhugh. Specificity of carbamate‐induced esterase inhibition in mice. Toxicol. Appl. Pharmacol. 6: 402–410, 1964.
 23. Bergmann, F., R. Segal, and S. Rimon. A new type of esterase in hog‐kidney extract. Biochem. J. 67: 481–486, 1957.
 24. Bridges, P. M. Absorption and metabolism of [14C]allethrin by the adult housefly, Musca domestica L. Biochem. J. 66: 316–320, 1957.
 25. Bull, D. L., and D. A. Lindquist. Metabolism of 3‐hydroxy‐N,N‐dimethyl crotonamide dimethyl phosphate by cotton plants, insects and rats. J. Agr. Food Chem. 12: 310–317, 1964.
 26. Bull, D. L., and D. A. Linquist. Metabolism of 3‐hydroxy‐N‐methyl‐cis‐crotonamide dimethyl phosphate (Azodrin) by insects and rats. J. Agr. Food Chem. 14: 105–109, 1966.
 27. Casida, J. E. Mode of action of carbamates. In: Annual Review of Entomology, edited by R. F. Smith. Palo Alto, Calif.: Ann. Rev., 1963, p. 39–58.
 28. Casida, J. E. (editor). Pyrethrum, the Natural Insecticide. New York: Academic Press, 1973.
 29. Casida, J. E., and K.‐B. Augustinsson. Reaction of plasma albumin with 1‐naphthyl N‐methylcarbamate and certain other esters. Biochim. Biophys. Acta 36: 411–426, 1959.
 30. Casida, J. E., E. C Kimmel, M. Elliott, and N. F. Janes. Oxidative metabolism of pyrethrins in mammals. Nature 230: 326–327, 1971.
 31. Casida, J. E., L. McBride, and R. P. Niedermeier. Metabolism of 2,2‐dichlorovinyl dimethyl phosphate in relation to residues in milk and mammalian tissues. J. Agr. Food Chem. 10: 370–377, 1962.
 32. Chamberlain, R. W. An investigation on the action of piperonyl butoxide with pyrethrum. Am. J. Hyg. 52: 153–183, 1950.
 33. Chamberlain, W. F., P. E. Gatterdam, and D. E. Hopkins. The metabolism of P32‐labeled dimethoate in sheep. J. Econ. Entomol. 54: 733–740, 1961.
 34. Chambon, P., M. Riotte, M. Daudon, R. Chambon‐Mougenot, and J. Bringuier. Etude du métabolisme des phthalates de dibutyle et de diéthyle chez le rat. Compt. Rend. 273: 2165–2168, 1971.
 35. Chen, P. R. S., and W. C. Dauterman. Studies on the toxicity of dimethoate analogs and their hydrolysis by sheep liver amidase. Pesticide Biochem. Physiol. 1: 340–348, 1971.
 36. Chen, P. R., W. P. Tucker, and W. C. Dauterman. Structure of biologically produced malathion monoacid. J. Agr. Food Chem. 17: 86–90, 1969.
 37. Chiu, Y. C., A. Hassan, F. E. Guthrie, and W. C. Dauterman. Studies on a series of branched‐chain analogs of diethyl malathion and malaoxon with regard to toxicity and in vitro enzymatic reactions. Toxicol. Appl. Pharmacol. 12: 219–228, 1968.
 38. Cochrane, D. R., J. D. Pope, H. P. Nicholson, and G. W. Bailey. The persistence of silvex in water and hydrosoils. Water Resources Res. 3: 517–523, 1967.
 39. Cohen, J. A., R. A. Oosterbaan, and M. G. P. J. Warringa. The turnover number of ali‐esterase, pseudo‐ and true cholinesterase and the combination of these enzymes with diisopropylfluorophosphate. Biochim. Biophys. Acta 18: 228–235, 1955.
 40. Cohen, J. A., R. A. Oosterbaan, H. S. Jansz, and F. Berends. The active site of esterases. J. Cellular Comp. Physiol. 54: 231–244, 1959.
 41. Cohen, J. A., and M. G. P. J. Warringa. Purification and properties of dialkylfluorophosphatase. Biochim. Biophys. Acta 26: 29–39, 1957.
 42. Cohen, S. D., J. E. Callaghan, and S. D. Murphy. Investigation of multiple mechanisms for potentiation of malaoxon's anticholinesterase action by triorthotolyl phosphate. Proc. Soc. Exptl. Biol. Med. 141: 906–910, 1972.
 43. Cohen, S. D., and S. D. Murphy. Comparative potentiation of malathion by triorthotolyl phosphate in four classes of vertebrates. Toxicol. Appl. Pharmacol. 16: 701–708, 1970.
 44. Cohen, S. D., and S. D. Murphy. Carboxylesterase inhibition as an indicator of malathion potentiation in mice. J. Pharmacol. Exptl. Therap. 176: 733–742, 1971.
 45. Cohen, S. D., and S. D. Murphy. Inactivation of malaoxon by mouse liver. Proc. Soc. Exptl. Biol. Med. 139: 1385–1389, 1972.
 46. Cook, J. W., J. R. Blake, and G. Yip. Malathionase. I. Activity and inhibition. J. Assoc. Offic. Agr. Chemists 41: 399–407, 1958.
 47. Cook, J. W., and G. Yip. Malathionase. II. Identity of a malathion metabolite. J. Assoc. Offic. Agr. Chemists 41: 407–411, 1958.
 48. Crafts, A. S. Evidence for hydrolysis of 2,4‐D during absorption by plants. Weeds 8: 19–25, 1960.
 49. Dauterman, W. C., and A. R. Main. Relationship between acute toxicity and in vitro inhibition and hydrolysis of a series of carbalkoxy homologs of malathion. Toxicol. Appl. Pharmacol. 9: 408–418, 1966.
 50. Dicowsky, L., and A. Morello. Glutathione‐dependent degradation of 2,2‐dichlorovinyl dimethyl phosphate (DDVP) by the rat. Life Sci., Part 2 10: 1031–1037, 1971.
 51. Dorough, H. W., and J. E. Casida. Nature of certain carbamate metabolites of the insecticide Sevin. J. Agr. Food Chem. 12: 294–304, 1964.
 52. Eason, L. H., and E. Stedman. Studies on the relationship between chemical constitution and physiological action. V. Molecular dissymmetry and physiological activity. Biochem. J. 27: 1257–1266, 1933.
 53. Ecobichon, D. J. Relative amounts of hepatic and renal carboxylesterases in mammalian species. Res. Commun. Chem. Pathol. Pharmacol. 3: 629–636, 1972.
 54. Ecobichon, D. J., and W. Kalow. Some properties of the soluble esterases of human liver. Can. J. Biochem. Physiol. 39: 1329–1332, 1961.
 55. Ecobichon, D. J., and W. Kalow. Properties and classification of the soluble esterases of human liver. Biochem. Pharmacol. 11: 573–583, 1962.
 56. Ecobichon, D. J., and W. Kalow. Action of organophosphorus compounds upon esterases of human liver. Can. J. Biochem. Physiol. 41: 1537–1546, 1963.
 57. Edelfrawi, M. E., and W. M. Hoskins. Relation of the rate of penetration and metabolism to the toxicity of sevin to three insect species. J. Econ. Entomol. 54: 401–405, 1961.
 58. Elliott, M. The relationship between the structure and the activity of pyrethroids. Bull. World Health Organ. 44: 315–324, 1971.
 59. Erdös, E. G., and L. E. Boggs. Hydrolysis of paraoxon in mammalian blood. Nature 190: 716–717, 1961.
 60. Erdös, E. G., C. R. Debay, and M. P. Westerman. Activation and inhibition of the arylesterase of human serum. Nature 184: 430–431, 1959.
 61. Erdös, E. G., C. R. Debay, and M. P. Westerman. Arylesterases in blood: effect of calcium and inhibitors. Biochem. Pharmacol. 5: 173–186, 1960.
 62. Erdös, E. G., and J. A. Laswick. Arylesterases in blood: Irreversible inactivation of the plasma enzyme. Biochem. Pharmacol. 8: 375–381, 1961.
 63. Fest, C., and K.‐J. Schmidt. The Chemistry of Organophosphorus Pesticides. New York: Springer‐Verlag, 1973.
 64. Fukunaga, K., J. Fukami, and T. Shishido. The in vitro metabolism of organophosphorus insecticides by tissue homogenates from mammals and insects. In: Residue Reviews, edited by F. A. Gunther. New York: Springer‐Verlag, 1969, vol. 25, p. 223–249.
 65. Fukuto, T. R., and R. L. Metcalf. Metabolism of insecticides in plants and animals. Ann. NY Acad. Sci. 160: 97–111, 1969.
 66. Goldstein, A. The mechanism of enzyme‐inhibitorsubstrate reactions. Illustrated by the cholinesterasephysostigmine‐acetylcholine system. J. Gen. Physiol. 27: 529–580, 1944.
 67. Goldstein, A. Properties and behaviors of purified human plasma cholinesterase. III. Competitive inhibition by prostigmine and other alkaloids with special reference to differences in kinetic behavior. Arch. Biochem. Biophys. 34: 169–188, 1951.
 68. Goldstein, A., and R. E. Hamslisch. Properties and behaviors of purified human plasma cholinesterase. IV. Enzymatic destruction of the inhibitors prostigmine and physostigmine. Arch. Biochem. Biophys. 35: 12–22, 1952.
 69. Goldstein, A., O. Krayer, M. A. Root, G. H. Acheson, and M. E. Doherty. Plasma neostigmine levels and cholinesterase inhibition in dogs and myasthenic patients. J. Pharmacol. Exptl. Therap. 96: 56–85, 1949.
 70. Goutier, R. Étude électrophorétique des estérases sériques et de la fixation du DF32P dans le sérum chez le lapin et le cobaye. Biochim. Biophys. Acta 19: 524–534, 1955.
 71. Guthrie, F. E., R. J. Monroe, and C. O. Abernathy. Response of the laboratory mouse to selection for resistance to insecticides. Toxicol. Appl. Pharmacol. 18: 92–101, 1971.
 72. Hassan, A., S. M. A. D. Zayed, and M. R. E. Bahig. Metabolism of organophosphorus insecticides. XI. Metabolic fate of dimethoate in the rat. Biochem. Pharmacol. 18: 2429–2438, 1969.
 73. Heath, D. F. Organophosphorus Poisons. Anticholinesterases and Related Compounds. New York: Pergamon Press, 1961.
 74. Hodgson, E., and J. E. Casida. Mammalian enzymes involved in the degradation of 2,2‐dichlorovinyl dimethyl phosphate. J. Agr. Food Chem. 10: 208–214, 1962.
 75. Hogan, J. W., and C. O. Knowles. Degradation of organophosphates by fish liver phosphatases. J. Fisheries Res. Board Can. 25: 1571–1579, 1968.
 76. Hollingworth, R. M. Comparative metabolism and selectivity of organophosphate and carbamate insecticides. Bull. World Health Organ. 44: 155–170, 1971.
 77. Holmstedt, B. Pharmacology of organophosphorus cholinesterase inhibitor. Pharmacol. Rev. 11: 567–688, 1959.
 78. Huggins, C., and J. Lapides. Chromogenic substrates. IV. Acyl esters of p‐nitrophenol as substrates for the colorimetric determination of esterases. J. Biol. Chem. 170: 467–482, 1947.
 79. Hutson, D. H., D. Blair, E. C. Hoadley, and B. A. Pickering. The metabolism of 14C‐Vapona in rats after administration by oral and inhalation routes. Toxicol. Appl. Pharmacol. 19: 378, 1971.
 80. Hutson, D. H., and E. C. Hoadley. The comparative metabolism of [14C‐vinyl]dichlorvos in animals and man. Arch. Toxikol. 30: 9–18, 1972.
 81. Hutson, D. H., and E. C. Hoadley. The metabolism of [14C‐methyl]dichlorvos in the rat and mouse. Xenobiotica 2: 107–116, 1972.
 82. Hutson, D. H., E. C. Hoadley, and B. A. Pickering. The metabolic fate of [vinyl‐1‐14C]dichlorvos in the rat after oral and inhalation exposure. Xenobiotica 1: 593–611, 1971.
 83. International Union of Biochemistry. Enzyme Nomenclature. Amsterdam: Elsevier, 1965.
 84. Jaeger, R. J., and R. J. Rubin. Plasticizers from plastic devices: extraction, metabolism and accumulation by biological systems. Science 170: 460–462, 1970.
 85. Johnsen, R. E., and P. A. Dahm. Activation and degradation efficiencies of liver microsomes from eight vertebrate species using organophosphates as substrates. J. Econ. Entomol. 59: 1437–1442, 1966.
 86. Johnson, M. K., and R. Lauwerys. Protection by some carbamates against the delayed neurotoxic effects of diisopropyl‐fluorophosphate. Nature 222: 1066–1067, 1969.
 87. Karczmar, A. G., O. Awad, and K. Blachut. Toxicity arising from joint intravenous administration of EPN and malathion to dogs. Toxicol. Appl. Pharmacol. 4: 133–147, 1962.
 88. Kearney, P. C. Purification and properties of an enzyme responsible for hydrolyzing phenylcarbamates. J. Agr. Food Chem. 13: 561–564, 1965.
 89. Knaak, J. B., and L. J. Sullivan. Metabolism of carbaryl in the dog. J. Agr. Food Chem. 15: 1125–1126, 1967.
 90. Knaak, J. B., M. J. Tullant, S. J. Kozbelt, and L. J. Sullivan. The metabolism of carbaryl in man, monkey, pig, and sheep. J. Agr. Food Chem. 16: 465–470, 1968.
 91. Kojima, K., and R. D. O'Brien. Paraoxon hydrolyzing enzymes in rat liver. J. Agr. Food Chem. 16: 574–584, 1968.
 92. Krishna, J. G., and J. E. Casida. Fate in rats of radiocarbon from ten variously labeled methyl and dimethylcrbamate‐14C insecticide chemicals and their hydrolysis products. J. Agr. Food Chem. 14: 98–105, 1966.
 93. Krueger, H. R., and J. E. Casida. Hydrolysis of certain organophosphate insecticides by housefly enzymes. J. Econ. Entomol. 54: 239–243, 1961.
 94. Krueger, H. R., and R. D. O'Brien. Relation between metabolism and differential toxicity of malathion in insects and mice. J. Econ. Entomol. 52: 1063–1067, 1959.
 95. Ku, T.‐Y. and J. L. Bishop. Penetration, excretion and metabolism of carbaryl in susceptible and resistant German cockroaches. J. Econ. Entomol. 60: 1328–1332, 1967.
 96. Lauwerys, R. R., and S. D. Murphy. Comparison of assay methods for studying O,O‐diethyl, O‐p‐nitrophenylphosphate (paraoxon) detoxication in vitro. Biochem. Pharmacol. 18: 789–800, 1969.
 97. Lauwerys, R. R., and S. D. Murphy. Interaction between paraoxon and tri‐o‐tolyl phosphate in rats. Toxicol. Appl. Pharmacol: 14: 348–357, 1969.
 98. Lee, D. H. K., and H. L. Falk (editors). Perspective on PAEs. In: Environ. Health Perspectives No. 3, Jan. 1973, p. 1–182. (U.S. Dept. Health, Educ., and Welfare Publ. No. NIH‐73‐218).
 99. Lichtenstein, E. P., T. W. Fuhremann, A. A. Hochberg, R. N. Zahlten, and F. W. Stratman. Metabolism of [14C]parathion and paraoxon with fractions and subfractions of rat liver cells. J. Agr. Food Chem. 21: 416–424, 1973.
 100. Lourteig, A., and C. E. Cardini. Action of lipases on some aromatic esters. Anales Farm Bioquim. Buenos Aires 18: 59–61, 1947.
 101. Lykken, L., and J. E. Casida. Metabolism of organic insecticide chemicals. Can. Med. Assoc. J. 100: 145–154, 1969.
 102. Main, A. R. The purification of the enzyme hydrolyzing diethyl p‐nitrophenyl phosphate (paraoxon) in sheep serum. Biochem. J. 74: 10–20, 1960.
 103. Main, A. R. Kinetics of active‐site‐directed irreversible inhibitions. In: Essays in Toxicology, edited by W. J. Hayes, Jr. New York: Academic Press, 1973, vol. 4, p. 59–105.
 104. Main, A. R., and P. E. Braid. Hydrolysis of malathion by aliesterase in vitro and in vivo. Biochem. J. 84: 255–263, 1962.
 105. Main, A. R., and W. C. Dauterman. Kinetics for the inhibition of carboxylesterase by malaoxon. Can. J. Biochem. 45: 757–771, 1967.
 106. March, R. B., T. R. Fukuto, R. L. Metcalf, and M. C. Maxon. Fate of P32 labeled malathion in the laying hen, white mouse and American cockroach. J. Econ. Entomol. 49: 185–195, 1956.
 107. Marton, A., and W. Kalow. Studies on aromatic esterase and cholinesterase of human serum. Can. J. Biochem. Physiol. 37: 1367–1373, 1959.
 108. Marton, A. V., and W. Kalow. Interaction between aromatic esterase of human serum and bivalent metal ions. Can. J. Biochem. Physiol. 40: 319–324, 1962.
 109. Matsumura, F., and A. W. A. Brown. Biochemistry of malathion resistance in Culex tarsalis. J. Econ. Entomol. 54: 1176–1185, 1961.
 110. Matsumura, F., and C. T. Ward. Degradation of insecticides by the human and rat liver. Arch. Environ. Health 13: 257–261, 1966.
 111. Mazur, A. An enzyme in animal tissues capable of hydrolyzing the phosphorus fluorine bond of alkyl fluorophosphates. J. Biol. Chem. 164: 271–289, 1946.
 112. Meagher, W. R. A heat labile insoluble conjugated form of 2,4‐dichlorophenoxyacetic acid and 2‐(2,4,5‐trichlorophenoxy)propionic acid in citrus peel. J. Agr. Food Chem. 14: 599–601, 1966.
 113. Melnikov, N. N. Chemistry of pesticides. In: Residue Reviews, edited by F. A. Gunther and J. D. Gunther. New York: Springer‐Verlag, 1971, vol. 36.
 114. Menzer, R. E., and W. C. Dauterman. Metabolism of some organophosphorus insecticides. J. Agr. Food Chem. 18: 1031–1037, 1970.
 115. Moore, D. J., and B. J. Rogers. The fate of long chain esters of 2,4‐D in plants. Weeds 8: 436–447, 1960.
 116. Mounter, L. A. Some studies of enzymatic effects of rabbit serum. J. Biol. Chem. 209: 813–817, 1954.
 117. Mounter, L. A. The complex nature of dialkylfluorophosphatases of hog and rat liver and kidney. J. Biol. Chem. 215: 705–711, 1955.
 118. Mounter, L. A. Metabolism of organophosphorus anticholinesterase agents. In: Handbuch der Experimentellen Pharmakologie, edited by O. Eichler and A. Farah. Berlin: Springer‐Verlag, 1963, vol. 15, p. 486–504.
 119. Mounter, L. A., H. C. Alexander, K. D. Tuck, and L. T. H. Dien. The pH dependence and dissociation constants of esterases and proteases treated with diisopropyl fluorophosphate. J. Biol. Chem. 226: 867–872, 1957.
 120. Mounter, L. A., R. F. Baxter, and A. Chanutin. Dialkylfluorophosphatases of microorganisms. J. Biol. Chem. 215: 699–704, 1955.
 121. Mounter, L. A., and A. Chanutin. Dialkylfluorophosphatase of kidney. II. Studies of activation and inhibition by metals. J. Biol. Chem. 204: 837–846, 1953.
 122. Mounter, L. A., and A. Chanutin. Dialkylfluorophosphatases of kidney. III. Studies of activation and inhibition by cofactors. J. Biol. Chem. 210: 219–226, 1954.
 123. Mounter, L. A., and L. T. H. Dien. Dialkylfluorophosphatases of kidney. V. The hydrolysis of organophosphorus compounds. J. Biol. Chem. 219: 685–690, 1956.
 124. Mounter, L. A., L. T. H. Dien, and A. Chanutin. The distribution of dialkylfluorophosphatases in the tissue of various species. J. Biol. Chem. 215: 691–697, 1955.
 125. Mounter, L. A., C. S. Floyd, and A. Chanutin. Dialkylfluorophosphatase of kidney. I. Purification and properties. J. Biol. Chem. 204: 221–232, 1953.
 126. Mounter, L. A., K. D. Tuck, H. C. Alexander, and L. T. H. Dien. The reactivity of esterases and proteases in the presence of organophosphorus compounds. J. Biol. Chem. 226: 873–879, 1957.
 127. Mounter, L. A., and V. P. Whittaker. The hydrolysis of esters of phenol by cholinesterases and other esterases. Biochem. J. 54: 551–559, 1953.
 128. Murphy, S. D. Liver metabolism and toxicity of thiophosphate insecticides in mammalian, avian and piscine species. Proc. Soc. Exptl. Biol. Med. 123: 392–398, 1966.
 129. Murphy, S. D. Malathion inhibition of esterases as a determinant of malathion toxicity. J. Pharmacol. Exptl. Therap. 156: 352–365, 1967.
 130. Murphy, S. D., R. L. Anderson, and K. P. Dubois. Potentiation of the toxicity of malathion by triorthotolylphosphate. Proc. Soc. Exptl. Biol. Med. 100: 483–487, 1959.
 131. Murphy, S. D., and K. L. Cheever. Feeding of insecticides Inhibition of carboxylesterase and cholinesterase activities in rats. Arch. Environ. Health 17: 249–758, 1968.
 132. Murphy, S. D., and K. P. DuBois. Quantitative measurement of inhibition of the enzyme detoxification of malathion by EPN (ethyl p‐nitrophenyl thiobenzenephosphonate). Proc. Soc. Exptl. Biol. Med. 96: 813–818, 1957.
 133. Myers, D. K. Competition of the aliesterase in rat serum with the pseudocholinesterase for diisopropyl fluorophosphate. Science 115: 568–570, 1952.
 134. Myers, D. K. Mechanism of the prophylactic action of diacetylmonoxime against sarin poisoning. Biochim. Biophys. Acta 34: 555–557, 1959.
 135. Myers, D. K., and A. Kemp. Inhibition of esterases by the fluorides of organic acids. Nature 173: 33–34, 1954.
 136. Neal, R. A., and K. P. DuBois. Studies on the mechanism of detoxification of cholinergic phosphorothioates. J. Pharmacol. Exptl. Therap. 148: 185–192, 1965.
 137. O'Brien, R. D. Properties and metabolism in the cockroach and mouse of malathion and malaoxon. J. Econ. Entomol. 50: 159–164, 1957.
 138. O'Brien, R. D. Toxic Phosphorus Esters. New York: Academic Press, 1960.
 139. O'Brien, R. D. Organophosphates and carbamates. In: Metabolic Inhibitors, edited by R. M. Hochster and J. H. Quastel. New York: Academic Press, 1963, vol. II, p. 207–241.
 140. O'Brien, R. D. Insecticides. Action and Metabolism. New York: Academic Press, 1967.
 141. O'Brien, R. D. Phosphorylation and carbamylation of cholinesterases. Ann. NY Acad. Sci. 160: 204–214, 1969.
 142. Plapp, F. W., W. S. Bigley, G. A. Chapman, and G. W. Eddy. Synergism of malathion against resistant houseflies and mosquitos. J. Econ. Entomol. 56: 643–649, 1963.
 143. Plapp, F. W., and G. W. Eddy. Synergism of malathion against resistant insects. Science 134: 2043–2044, 1961.
 144. Polak, R. L., and E. M. Cohen. The influence of triorthocresylphosphate on the distribution of 32P in the body of the rat after the injection of 32P‐sarin. Biochem. Pharmacol. 18: 813–820, 1969.
 145. Ramachandran, B. V., and G. Agren. Esterases of ratliver cell fractions. Correlation of DF32P‐binding capacity to esterase activity. Biochem. Pharmacol. 12: 981–988, 1963.
 146. Ramachandran, B. V., and G. Agren. Determination of DFPase in rabbit and rat tissues using DF32P. Biochem. Pharmacol. 13: 849–854, 1964.
 147. Reed, W. D., and T. R. Jukuto. The reactivation of carbamate‐inhibited cholinesterase, kinetic parameters. Pesticide Biochem. Physiol. 3: 120–130, 1973.
 148. Reiner, E. Spontaneous reactivation of phosphorylated and carbamylated cholinesterases. Bull. World Health Organ. 44: 109–112, 1971.
 149. Reiner, E., and W. N. Aldridge. Effect of pH on inhibition and spontaneous reactivation of acetylcholinesterase treated with esters of phosphorus acids and of carbamic acids. Biochem. J. 105: 171–179, 1967.
 150. Ryan, A. J. The metabolism of pesticidal carbamates. C.R.C. Critical Rev. Toxicol. 1: 33–54, 1971.
 151. Schaffer, C. B., C. P. Carpenter, and H. F. Smyth. Acute and subacute toxicity of di‐(2‐ethylhexyl)phthalate with note upon its metabolism. J. Ind. Hyg. Toxicol. 27: 130–135, 1945.
 152. Seume, F. W., and R. D. O'Brien. Potentiation of the toxicity to insects and mice of phosphorothionates containing carboxyester and carboxyamide groups. Toxicol. Appl. Pharmacol. 2: 495–503, 1960.
 153. Smith, C. C. Toxicity of butyl stearate, dibutyl sebacate dibutyl phthalate and methoxyethyl oleate. Arch. Ind. Hyg. Occupational Med. 7: 310–318, 1953.
 154. St. John, L. E., Jr., D. G. Wagner, and D. J. Lisk. Fate of atrazine, kuron, silvex and 2,4,5‐T in the dairy cow. J. Dairy Sci. 47: 1267–1270, 1964.
 155. Tove, S. B. The esterolytic activity of serum albumin. Biochim. Biophys. Acta 57: 230–235, 1962.
 156. Triolo, A. J., E. Mata, and J. M. Coon. Effects of organochlorine insecticides on the toxicity and in vitro plasma detoxication of paraoxon. Toxicol. Appl. Pharmacol. 17: 174–180, 1970.
 157. Uchida, T., W. C. Dauterman, and R. D. O'Brien. The metabolism of dimethoate by vertebrate tissue. J. Agr. Food Chem. 12: 48–52, 1964.
 158. Uchida, T., and R. D. O'Brien. Dimethoate degradation by human liver and its significance for acute toxicity. Toxicol. Appl. Pharmacol. 10: 89–94, 1967.
 159. Uchida, T., H. S. Rahmati, and R. D. O'Brien. The penetration and metabolism of H3‐dimethoate in insects. J. Econ. Entomol. 58: 831–835, 1965.
 160. Uchida, T., J. Zchintzsch, and R. D. O'Brien. Relation between synergism and metabolism of dimethoate in mammals and insects. Toxicol. Appl. Pharmacol. 8: 259–265, 1966.
 161. Welling, W., P. Blaakmeer, G. J. Vink, and S. Voerman. In vitro hydrolysis of paraoxon by parathion resistant houseflies. Pesticide Biochem. Physiol. 1: 61–70, 1973.
 162. Wheeler, L., and A. Strother. In vitro metabolism of the N‐methylcarbamates Zectran and Mesurol by liver, kidney, and blood of dogs and rats. J. Pharmacol. Exptl. Therap. 178: 371–382, 1971.
 163. Whitehouse, L. W., and D. J. Ecobichon. Paraoxon formation and hydrolysis by mammalian liver. Pesticide Biochem. Physiol. 5: 314–322, 1975.
 164. Wilde, C. E., and R. G. O. Kekwick. The arylesterases of human serum. Biochem. J. 91: 297–307, 1964.
 165. winteringham, F. P. W., A. Harrison, and P. M. Bridges. Absorption and metabolism of [14HC]pyrethroids by the adult housefly Musca domeestica L. in vivo. Biochem. J. 61: 359–367, 1955.
 166. Yamamoto, I., M. Elliott, and J. E. Casida. The metabolic fate of pyrethrin I, pyrethrin II and allethrin. Bull. World Health Organ. 44: 347–348, 1971.
 167. Yip, G., and J. W. Cook. Malathionase. III. Substrate specificity studies. J. Assoc. Offic. Agr. Chemists 42: 405–407, 1959.
 168. Zeller, E. A., G. A. Fleisher, R. A. McNaughton, and J. C. Schweppe. New substrates for cholinesterases. Proc. Soc. Exptl. Biol. Med. 71: 526–529, 1949.

Contact Editor

Submit a note to the editor about this article by filling in the form below.

* Required Field

How to Cite

D. J. Ecobichon. Hydrolytic Transformation of Environmental Pollutants. Compr Physiol 2011, Supplement 26: Handbook of Physiology, Reactions to Environmental Agents: 441-454. First published in print 1977. doi: 10.1002/cphy.cp090127