Comparative Analysis of Glyoxylate Cycle Key Enzyme Isocitrate Lyase from Organisms of Different Systematic Groups
Isocitrate lyase and malate synthase are the key enzymes of glyoxylate cycle that represents the most important stage on the pathway of conversion of fatty acids to carbohydrates. Until now, induction of enzymes of this metabolic pathway was considered to take place only in cells of prokaryotes, plants, fungi, and nematodes in response to arising demands in carbohydrates. However, the isocitrate lyase activities have been detected in the liver of food-starved rats in our previous work and in pupas of the butterfly Papilio machaon in the present study. The enzymes from both studied objects were purified to homogeneous condition. The main kinetic and physicochemical properties of isocitrate lyase were studied. Organisms of evolutionary distant taxa—mammal, insect, and plant—were chosen for comparative analysis of properties of the studied enzyme. A substantial similarity of kinetic and physicochemical properties of plant and animal isocitrate leases has been found. At the same time, the absence of specific for prokaryotic, plant, and nematode isocitrate lyase nucleotide sequences has been established in mRNA from liver of starved rats and swallowtail pupa. These results are completely confirmed by analysis of the complete genome sequences of the mouse, Drosophila, and human. The obtained data raise the question about the pathway of evolution of genes of the glyoxylate cycle key enzymes.
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- 3.Zemlyanukhin, A.A., Zemlyanukhin, L.A., Eprintsev, A.T., and Igamberdiev, A.U., Glioksilatnyi Tsikl Rastenii (The Glyoxylate Cycle of Plants), Voronezh, 1986.Google Scholar
- 5.Tishchenko, B.P., Fisiologiya Nasekomykh (Insects Physiology), Moscow, 1986.Google Scholar
- 6.Kamel, M.Y. and Fahmy, A.S., Biochemical Studies of Tick Embryogenesis. V. Purification and Partial Characterization of Isocitrate Lyase from Eggs of the Tick Hyalomma dromedarii, Comp. Biochem. Physiol., 1982, vol. 72B, pp. 107–115.Google Scholar
- 7.Benevides, J.M., Tremblay, G.C., and Hammen, C.S., Determination of Isocitrate Lyase and Malate Synthase Activities in a Marine Mollusk by a New Method of Assay, Comp. pBiochem. Physiol., 1989, vol. 94B, pp. 779–782.Google Scholar
- 9.Davis, W.L., Jones, R.G., Farmer, G.R., Dickerson, T., Cortinas, E., Cooper, O.J., Crawford, L.A., and Goodman, D.B., Identification of Glyoxylate Cycle Enzymes in Chick Liver—The Effect of Vitamin D3: Cytochemistry and Biochemistry, Anat. Rec., 1990, vol. 227, pp. 271–284.CrossRefPubMedGoogle Scholar
- 11.Lebkova, N.P., Current Concepts of Intracellular Mechanisms of Energy Maintenance in Norm and Pathology, Vestn. RAMN, 2000, vol. 9, pp. 16–22.Google Scholar
- 13.Popov, V.N., Volvenkin, S.V., Eprintsev, A.E., and Igamberdiev, A.U., Induction of Glyoxylate Cycle Enzymes in Various Tissues of Starving Rats, Izv. RAN, Ser. Biol., 2000, vol. 6, pp. 672–678.Google Scholar
- 14.Popov, V.N., Igamberdiev, A.U., and Volvenkin, S.V., Purification and Properties of Isocitrate Lyase and Malate Synthase from Fasting Rat Liver, Biokhimiya, 1996, vol. 61, pp. 1898–1903.Google Scholar
- 17.Dixon, G.H. and Kornberg, H.L., Assay Methods for the Key Enzymes of the Glyoxylate Cycle, Biochem. J., 1959, vol. 72, p. 3.Google Scholar
- 24.Zemlyanukhin, A.A., Igamberdiev, A.U., and Presnyakova, E.N., Purification and Characterization of Isocitrate Lyase from Maize Scutella, Biokhimiya, 1986, vol. 51, pp. 442–448.Google Scholar
- 25.Dixon, M. and Webb, E., Fermenty (Enzymes), Moscow, 1982. See also: Dixon, M. and Webb, E.C., Enzyme, 3rd Ed., Longmans, London, 1979.Google Scholar
- 26.Koolman, J. and Rohm, K.-H., Naglyadnaya Biokhimiya (Demonstrative Biochemistry), Moscow, 2000. See also: Koolman, J. and Rohm, K.-H., Taschenatlas der Biochemie, Georg Thieme Verlag Stuttgatr, New York, 1998.Google Scholar