Macromolecular Compartmentation and Channeling

International Review of Cytology

Volumn 192, Issue , 1999, Pages 255-280

  Ovádi, Judit ^a   Srere, Paul A ^a,b  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b VA NORTH TEXAS HEALTH CARE SYSTEM   (United States)

Author keywords

Ambiquity; Channeling; Enzyme structure protein interactions; Enzyme enzyme interactions; Metabolism

Indexed keywords

ENZYME; STRUCTURAL PROTEIN;

CELL COMPARTMENTALIZATION; CELL METABOLISM; COMPLEX FORMATION; ENZYME KINETICS; MACROMOLECULE; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; REVIEW;

EID: 0033991699     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0074-7696(08)60529-x     Document Type: Article

References (79)

1. Agius, L., and Sherratt, H. S. A. (1996). "Channelling in Intermediary Metabolism." Portland Press, London.
2. Agutter, P. S. (1990). "Between Nucleus and Cytoplasm." Chapman & Hall, London.
3. Backman, L., and Johansson, G. (1976). Enzyme-enzyme complexes between aspartate aminotransferase and malate dehydrogenase from pig heart muscle. FEBS Lett. 65, 39-43.
4. Beeckmans S., and Kanarek, L. (1981). Demonstration of physical interactions between consecutive enzymes of the citric acid cycle and of the aspartate-malate shuttle: A study involving fumarase, malate dehydrogenase, citrate synthase and aspartate aminotransferase. Eur. J. Biochem. 117, 527-535.
5. Beeckmans, S., Van Driessche, E., and Kanarek, L. (1989). The visualization by affinity electrophoresis of a specific association between the consecutive citric acid cycle enzymes fumarase and malate dehydrogenase. Eur. J. Biochem. 183, 449-454.
6. Berry, M. N., Gregory, R. B., Grivell, A. R., Henly, D. C, Philips, J. W., Wallace, P. G., and Welch, G. R. (1987). Linear relationships between mitochondrial forces and cytoplasmic flows argue for the organized energy-coupled nature of cellular metabolism. FEBS Lett. 224, 201-207.
7. Berry, M. N., Gregory, R. B., Grivell, A. R., Henly, D. C., Nobes, C. D., Philips, J. W., and Wallace, P. G. (1988). Intracellular mitochondrial membrane potential as an indicator of hepatocytes energy metabolism: Further evidence for thermodynamic control of mechanism. Biochim. Biophys. Acta 936, 294-306.
8. Billow, L. (1987). Characterization of an artificial bifunctional enzyme β-galactosidase/galactokinase prepared by gene fusion. Eur. J. Biochem. 163, 443-448.
9. Clarke, F., Stephan, P., Morton, D., and Weidemann, J. (1983). The role of actin and associated structural proteins in the organization of glycolytic enzymes. In "Actin: Structure and Function in Muscle and Non-muscle Cells" (J. Barden, and C. Dos Remedios, eds.), pp. 249-257. Academic Press, Sidney.
10. Clarke, F. M., and Masters, C. J. (1976). Interactions between muscle proteins and glycolytic enzymes. Int. J. Biochem. 7, 359-365.
11. Dolken, G., Leisner, E., and Pette, D. (1975). Immunofluorescent localization of glycogenolytic and glycolytic enzyme proteins and of malate dehydrogenase isozymes in cross-triated muscle and heart of the rabbit. Histochemistry 43, 113-121.
12. D'Souza, S. F., and Srere, P. A. (1983). Cross-linking of mitochondrial matrix proteins in situ. Biochim. Biophys. Acta 724, 40-51.
13. Elcock, A. H., and McCammon, J. A. (1996). Evidence for electrostatic channeling in a fusion protein of malate dehydrogenase and citrate synthase. Biochemistry 35, 12652-12658.
14. Fahien, L. A., and Chobanian, M. C. (1997). Kinetic advantages of multienzyme complexes involving aminotransferases. In "Channeling in Intermediary Metabolism" (L. Agius and H. S. A. Sherratt, eds.), pp. 219-236. Portland Press, London.
15. Fahien, L. A., and Kmiotek, E. (1979). Precipitation of complex between glutamate dehydrogenase and mitochondrial enzymes. J. Biol. Chem. 254, 5983.
16. Fahien, L. A., MacDonald, M. J., Teller, J. K., Fibich, B., and Fahien, C. M. (1989). Kinetic advantages of hetero-enzyme complexes with glutamate dehydrogenase and the αketoglutarate dehydrogenase complex. J. Biol. Chem. 264, 12303-12312.
17. Goldman, R., and Katchalski, E. (1971). Kinetic behavior of a two-enzyme membrane carrying out a consecutive set of reactions. J. Theor. Biol. 32, 243-257.
18. Halper, L. A., and Srere, P. A. (1977). Interaction between citrate synthase and mitochondrial malate dehydrogenase in the presence of polyethylene glycol. Arch. Biochem. Biophys. 184, 529-534.
19. 13C NMR. J. Mol. Cell. Cardiol. 26, 1197-1210.
20. Hardin, C. D., and Robers, T. M. (1995). Compartmentation of glucose and fructose 1,6-bisphosphate metabolism in vascular smooth muscle. Biochemistry 34, 1323-1331.
21. Hasselbeck, R. J., and McAlister-Henn, L. (1993). Function and expression of yeast mitochondrial NAD- and NADP-specific isocitrate dehydrogenases. J. Biol. Chem. 268, 12116-12122.
22. Hervé, G., Nagy, M., LeGouar, M., Penverne, B., and Ladjimi, M. (1993). The carbamoyl phosphate synthase-aspartate transcarbamoylase complex of Saccharomyces cerevisiae: Molecular and cellular aspects. Biochem. Soc. Trans. 21, 195-198.
23. Hesketh, J. E., and Pryme, I. F. (1991). Interaction between mRNA, ribosomes and the cytoskeleton. Biochem. J. 277, 1-10.
24. Home, Z., and Hesketh, J. E. (1990). Immunological localization of ribosomes in striated rat muscle. Biochem. J. 268, 231-236.
25. Humphreys, L., Reid, S., and Masters, C. J. (1986). Studies on the topographical localization of the binding sites for substrate and for actin on the enzymes, glyceraldehyde phosphate dehydrogenase and phosphofructokinase. Int. J. Biochem. 18, 445-451.
26. Hyde, C. C, Ahmed, S. A., Padlan, E. A., Miles, E. W., and Davies, D. R. (1988). Three-dimensional structure of the tryptophan synthase a2b2 multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263, 7857-7871.
27. Keleti, T., Ovádi, J., and Batke, J. (1989). Kinetic and physico-chemical analysis of enzyme complexes and their possible role in the control of metabolism. Prog. Biophys. Molec. Biol. 53, 105-152.
28. Knull, H. R., and Walsh, J. L. (1992). Association of glycolytic enzymes with the cytoskeleton. Curr. Top. Cell. Regul. 33, 15-30.
29. Lindbladh, C., Persson, M., Búlow, L., and Mosbach, K. (1992). Characterization of a recombinant bifunctional enzyme, galactose dehydrogenase/bacterial luciferase, displaying an improved bioluminescence in a three-enzyme system. Eur. J. Biochem. 204, 241-247.
30. Lindbladh, C., Brodeur, R. D., Small, W. C, Lilius, G., Bülow, L., Mosbach, K., and Srere, P. A. (1994a). Metabolic studies on S. cerevisiae containing fused citrate synthase/malate dehydrogenase. Biochemistry 33, 11684-11691.
31. Lindbladh, C., Rault, M., Hagglund, C, Small, W. C., Mosbach, K., Bülow, L., Evans, C, and Srere, P. A. (1994b). Preparation and kinetic characterization of a fusion protein of yeast mitochondrial citrate synthase and malate dehydrogenase. Biochemistry 33, 11692-11698.
32. Low, P. S., Rathinavelu, P., and Harrison, M. L. (1993). Regulation of glycolysis via reversible enzyme binding to the membrane protein, Band 3. J. Biol. Chem. 268, 14627-14631.
33. Masters, C. J. (1981). Interactions between soluble enzymes and subcellular structure. CRC Crit. Rev. Biochem. 11, 105-143.
34. Masters, C. J. (1984). Interactions between glycolytic enzymes and components of the cytomatrix. J. Cell Biol. 99, 222S-225S.
35. Meek, T. D., Garvey, E. R., and Santi, D. V. (1985). Purification and characterization of the bifunctional thymidylate synthase-dihydrofolate reductase from methotrexate-resistant Leishmania tropica. Biochemistry 24, 678-686.
36. Méjean, C, Pons, F., Benyamin, Y., and Roustan, C. (1989). Antigenic probes locate binding sites for the glycolytic enzymes gIyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments. Biochem. J. 264, 671-677.
37. Minaschek, G., Stewart, U. G., Blum, S., and Bereiter-Hahn, J. (1992). Microcompartmentation of glycolytic enzymes in cultured cells. Eur. J. Cell Biol. 58, 418-428.
38. Nagy, E., and Rigby, W. F. (1995). Glyceraldehyde-3-phosphate dehydrogenase selectively binds AU-rich RNA in the NAD(+)-binding region (Rossmann fold). J. Biol. Chem. 270, 2755-2763.
39. Negrutskii, B. S., and Deutscher, M. P. (1991). Channeling of aminoacyl-tRNA for protein synthesis in vivo. Proc. Natl. Acad. Sci. U.S.A. 88, 4991-4995.
40. Oblinger, M. M., Foe, L. G., Kwiatkowska, D., and Kemp, R. G. (1988). Phosphofructokinase in the rat nervous system: Regional differences in activity and characteristics of axonal transport. J. Neurosci. Res. 21, 25-34.
41. Orosz, F., and Ovádi, J. (1987). A simple approach to identify the mechanism of intermediate transfer: Enzyme system related to triose phosphate metabolism. Biochim. Biophys. Acta 915, 53-59.
42. Orosz, F., Christova, T. Y., and Ovádi, J. (1987). Aldolase decreases the dissociation-induced inactivation of muscle phosphofructokinase. Biochem. Biophys. Res. Commun. 147,11211128.
43. Ovádi, J. (1995). "Cell Architecture and Metabolic Channeling," Molecular Biology Intelligence Unit. R.G. Landes and Springer-Verlag, New York and Berlin.
44. Ovádi, J., Huang, Y., and Spivey, H. O. (1994). Binding of malate dehydrogenase and NADH channeling to Complex I. J. Mol. Recognition, 7, 265-273.
45. Pagliaro, L., and Taylor, D. L. (1992). 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells. J. Cell Biol. 118, 859-863.
46. Pagliaro, L., Kerr, K., and Taylor, D. L. (1989). Enolase exists in the fluid phase of 3T3 cells. J. Cell Sci. 94, 333-342.
47. Penverne, B., Belkaid, M., and Hervé, G. (1994). In situ behavior of the pyrimidine pathway enzymes in Saccharomyces cerevisiae. 4. The channelling of carbamylphosphate to aspartate transcarbamylase and its partition in the pyrimidine and arginine pathways. Arch. Biochein. Biophys. 309, 85-93.
48. Persson, L.-O., and Srere, P. A. (1992). Purification of the mitochondrial citrate transporter in yeast. Biochem. Biophys. Res. Commun. 183, 70-76.
49. Porpaczy, Z., Sümegi, B., and Alkonyi, I. (1983). Association between the α-ketoglutarate dehydrogenase complex and succinate thiokinase. Biochim. Biophys. Acta 749, 172-179.
50. Porpaczy, Z., Siimegi, B., and Alkonyi, I. (1987). Interaction between NAD-dependent isocitrate dehydrogenase, α-ketoglutarate dehydrogenase complex, and NADH:ubiquinone oxidoreductase. J. Biol. Chem. 262, 9509-9514.
51. Rabinowitz, M. (1996). Uncharged tRNA-phosphofructokinase interaction in amino acid deficiency. Amino Acids 10, 99-108.
52. Robinson, J. B., Jr., and Srere, P. A. (1985). Organization of Krebs tricarboxylic acid cycle enzymes in mitochondria. J. Biol. Chem. 260, 10800-10805.
53. Robinson, J. B., Jr., Inman, L., Sümegi, B., and Srere, P. A. (1987). Further characterization of the Krebs Tricarboxylic acid cycle metabolon. J. Biol. Chem. 262, 1786-1790.
54. Ryazanov, A. G. (1988). Organization of soluble enzymes in the cell. Relay at the surface. FEBS Lett. 373, 1-4.
55. Ryazanov, A. G., Ashmarina, L. I., and Murinetz, V. I. (1988). Association of glyceraldehyde-3-phosphate dehydrogenase with mono-and polyribosomes of rabbit reticulocytes. Eur. J. Biochem. 171, 301-305.
56. Sherry, A. D., Siimegi, B., Miller, B., Cottam, G. L., Gawa, S., Jones, J. G., and Malloy, C. R. (1994). Orientation-conserved transfer of symmetric Krebs cycle intermediates in mammalian tissue. Biochemistry 33, 6268-6275.
57. Singer, R. H., Langevin, G. L., and Lawrence, J. B. (1989). Ultrastructural visualization of cytoskeletal mRNAs and their associated proteins using double-label in situ hybridization. J. Cell Dial. 108, 2343-2353.
58. Somero, G. N., and Hand, S. C. (1990). Protein assembly and metabolic regulation: Physiological and evolutionary perspectives. Physiol. Zool. 63, 443-471.
59. Spirin, A. S., and Ajtkozhin, M. A. (1985). Informosomes and polyribosome-associated proteins in eucaryotes. Trends Biochem. Sci. 10,162-165.
60. Srere, P. A. (1981). Protein crystals as a model for mitochondrial matrix proteins. Trends Biochem. Sci. 6, 4-7.
61. Srere, P. A., and Mosbach, K. (1974). Metabolic compartmentation: Symbiotic, organellar, multienzymic, and microenvironmental. Anna. Rev. Microbiol. 28, 61-83.
62. Srere, P. A., Mattiasson, B., and Mosbach, K. (1973). An immobilized three-enzyme system: A model for microenvironmental compartmentation in mitochondria. Proc. Natl. Acad. Sci. U.S.A. 70, 2534-2538.
63. Srivastava, D. K., And Bernhard, S. A. (1985). The mechanism of transfer of NADH dehydrogenases. Biochemistry 24, 623-628.
64. Srivastava, D. K., and Berhard, S. A. (1987). Biophysical chemistry of metabolic reaction sequences in concentrated enzyme solution and in the cell. Anna. Rev. Biophys. Biophys. Chem. 16, 175-204.
65. Sumegi, B., and Alkonyi, I. (1983). A study on the physical interaction between the pyruvate dehydrogenase complex and citrate synthase. Biochim. Biophys. Acta 749, 163-171.
66. Sümegi, B., and Srere, P. A. (1984b). Complex I binds several mitochondrial NAD-coupled dehydrogenases. J. Biol. Chem. 259, 15040-15045.
67. S̈megi, B., Gilbert, H. F., and Srere, P. A, (1985). Interaction between citrate synthase and thiolase. J. Biol. Chem. 260, 188-190.
68. S̈megi, B., Sherry, A. D., and Malloy, C. R. (1990). Channeling of TCA cycle intermediates in cultured Saccharomyces cerevisiae. Biochemistry 29, 9106-9110.
69. S̈megi, B., Porpaczy, Z., McCammon, M. T., Sherry, A. D., Malloy, C. R., and Srere, P. A. (1992). Regulatory consequences of organization of citric acid cycle enzymes. Curr. Top. Cell. Regul. 33, 249-260.
70. I3C NMR studies. Biochemistry 32, 12725-12729.
71. Tompa, P., Batke, J., Ovádi, J., Welch, G. R., and Srere, P. A. (1987). Quantitation of the interaction between citrate synthase and malate dehydrogenase. J. Biol. Chem. 262, 6089-6092.
72. Trujillo, M., Donald, R. G. K., Roos, D. S., Greene, P. J., and Santi, D. V. (1996). Heterologous expression and characterization of the bifunctional dihydrofolate reductase-thymidylate synthase enzyme of Toxoplasma gondii. Biochemistry 35, 6366-6374.
73. Tyiska, R. L., Williams, J. S., Brent, L. G., Hudson, A. P., Clark, B. J., Robinson, J. B., Jr., and Srere, P. A. (1986). Interactions of matrix enzyme activities with mitochondrial inner membranes. NATO Series A: Life Sciences, vol. 127, pp. 177-189, Plenum Press, New York.
74. Ureta, T. (1991). The role of isoenzymes in metabolite channeling. J. Theor. Biol. 152, 81-84.
75. Vértessy, B. G., Orosz, F., and Ovádi, J. (1991). Modulation of interaction between aldolase and glycerol-phosphate dehydrogenase by fructose phosphates. Biochim. Biophys. Acta. 1078, 236-242.
76. Vértessy, B. G., Orosz, F., Kovács, J., and Ovádi, J. (1997). Alternative binding of two sequential glycolytic enzymes to microtubules: Molecular studies in phosphofructokinase/ aldolase/microtubule system. J. Biol. Chem. 272, 25542-25546.
77. Welch, G. R. (1977). On the role of organized multienzyme systems in cellular metabolism: A general synthesis. Prog- Biophys. Mol. Biol. 32, 103-191.
78. Wilson, J. E. (1978). Ambiquitous enzymes: Variation in intracellular distribution as a regulatory mechanism. Trends Biochem. Sci. 3, 124-125.
79. Wilson, J. E. (1980). Brain hexokinase, the prototype ambiquitous enzyme. Curr. Top. Cell. Regul. 16, 1-54.