Abstract
Carbonyl reduction is a metabolic pathway being widely distributed in living matter and many endogenous compounds such as prostaglandins, biogenic amines and steroids, as well as xenobiotic aromatic and aliphatic aldehydes and ketones are converted to the corresponding alcohols prior to their further metabolism and/or elimination (Felsted and Bachur, 1980). The enzymes mediating carbonyl reduction belong to the aldo-keto reductase family and comprise carbonyl reductase (EC 1.1.1.184), aldehyde reductase (EC 1.1.1.2) and aldose reductase (EC 1.1.1.21), which share common features such as monomelic structure (30–40 kDa), cytosolic subcellular localization and a cosubstrate specificity for NADPH (Wermuth, 1985). Furthermore, enzymes like dihydrodiol dehydrogenase (EC 1.3.1.20) and hydroxysteroid dehydrogenases (3α-, 3ß-, 17ß-) were also shown to be involved in reductive metabolism of carbonyl compounds or, as has been supposed, isozymes of the latter two groups might even be identical to enzymes described previously as aldo-keto reductases (Pietruszko and Chen, 1976; Penning et al., 1984; Sawada et al., 1988).
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References
Ahmed, N.K., Felsted, R.L., and Bachur, N.R., 1979, Comparison and characterization of mammalian xenobiotic ketone reductases, J. Pharmacol Exp. Ther. 209: 12.
Ansorge, W., 1985, Fast and sensitive detection of protein and DNA bands by treatment with potassium permanganate J. Biochem. Biophys. Meth. 11: 13.
Bradford, M.M., 1976, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72: 248.
Felsted, R.L. and Bachur, N.R., 1980, Mammalian carbonyl reductases, Drug Metab. Rev. 11: 1.
Hara, A., Usui, S., Hayashibara, M., Horiuchi, T., Nakayama, T., and Sawada, H., 1987, Microsomal carbonyl reductase in rat liver. Sex difference, hormonal regulation and characterization, in: “Enzymology and Molecular Biology of Carbonyl Metabolism,” H. Weiner and T.G. Flynn, eds., Alan R. Liss, New York, p. 401.
Kahl, G.F., 1970, Experiments on the metyrapone reducing microsomal enzyme system, Naunyn-Schmiedebergs Arch. Pharmacol. 266: 61.
Kling, L., Legrum, W., and Netter, K.J., 1985, Induction of liver cytochrome P-450 in mice by warfarin, Biochem. Pharmacol. 34: 85.
Laemmli, U.K., 1970, Cleavage of structural proteins during the assembly of the head of bacterophage T4, Nature 227: 680.
Lakshmi, V. and Monder, C., 1988, Purification and characterization of the corticosteroid 11ß-dehydrogenase component of the rat liver 11ß-hydroxysteroid dehydrogenase complex, Endocrinology 123: 2390.
Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J., 1951, Protein measurements with the Folin phenol reagent, J. Biol. Chem. 193: 265.
Maser, E. and Legrum, W., 1985, Alteration of the inhibitory effect of metyrapone by reduction to metyrapol during the metabolism of methacetin in vivo in mice, Naunyn-Schmiedeberg’s Arch. Pharmacol. 331: 283.
Maser, E. and Netter, K.J., 1989, Purification and properties of a metyrapone reducing enzyme from mouse liver microsomes — this ketone is reduced by an aldehyde reductase, Biochem. Pharmacol. 38: 3049.
Maser, E. and Netter, K.J., 1991, Reductive metabolism of metyrapone by a quercitrin-sensitive ketone reductase in mouse liver cytosol, Biochem. Pharmacol. 41: 1595.
Maser, E., Oppermann, U., Bannenberg, G., and Netter, K.J., 1992, Functional and immunological relationships between metyrapone reductase from mouse liver microsomes and 3α-hydroxysteroid dehydrogenase from Pseudomonas testosteroni, FEBS Lett. 297: 196.
Maser, E., Gebel, T., and Netter, K.J., 1991, Carbonyl reduction of metyrapone in human liver, Biochem. Pharmacol. 42: S93.
Nakagawa, M., Tsukada, F., Nakayama, T., Matsuura, K., Hara, A., and Sawada, H., 1989, Identification of two dihydrodiol dehydrogenases associated with 3(17)α-hydroxysteroid dehydrogenase activity in mouse kidney, J. Biochem. 106: 633.
Penning, T.M., Mukharji, I., Barrows, S., and Talalay, P., 1984, Purification and properties of a 3α-hydroxysteroid dehydrogenase of rat liver cytosol and its inhibition by anti-inflammatory drugs, Biochem. J. 222: 601.
Pietruszko, R. and Chen, F.F., 1976, Aldehyde reductase from rat liver is a 3α-hydroxysteroid dehydrogenase, Biochem. Pharmacol. 25: 2721.
Sawada, H. and Hara, A., 1978, Studies on metabolism of bromazepam, Drug Metab. Dispos. 6: 205.
Sawada, H., Hara, A., Hayashibara, M., and Nakayama, T., 1979, Guinea pig liver aromatic aldehyde-ketone reductases identical with 17ß-hydroxysteroid dehydrogenase isozymes, J. Biochem. Tokyo 86: 883.
Sawada, H., Hara, A., Hayashibara, M., Nakayama, T., Usui, S., and Saeki, T., 1981, Microsomal reductase for aromatic aldehydes and ketones in guinea pig liver. Purification, characterization, and functional relationship to hexose-6-phosphate dehydrogenase, J. Biochem. 90: 1077.
Sawada, H., Hara, A., Nakayama, T., Nakagawa, M., Inoue, Y., Hasebe, K., and Zhang, Y., 1988, Mouse liver dihydrodiol dehydrogenases: identity of the predominant and a minor form with 17ß-hydroxysteroid dehydrogenase and aldehyde reductase, Biochem. Pharmacol. 37: 453.
Usansky, J.I. and Damani, L.A., 1985, The in vivo metabolism of metyrapone in the rat, in: “Biological Oxidation of Nitrogen in Organic Molecules,” J.W. Gorrod and L.A. Damani, eds., Ellis Horwood, Chichester, p. 231.
Usui, S., Hara, A., Nakayama, T., and Sawada, H., 1984, Purification and characterization of two forms of microsomal carbonyl reductase in guinea pig liver, Biochem. J. 223: 697.
Wermuth, B., 1985, Aldo-keto reductases, in: “Enzymology of Carbonyl Metabolism 2”, T.G. Flynn and H. Weiner, eds., Alan R. Liss, New York, p. 209.
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© 1993 Springer Science+Business Media New York
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Maser, E. (1993). The Purification and Properties of a Novel Carbonyl Reducing Enzyme from Mouse Liver Microsomes. In: Weiner, H., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 4. Advances in Experimental Medicine and Biology, vol 328. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2904-0_36
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DOI: https://doi.org/10.1007/978-1-4615-2904-0_36
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