Interaction between mammalian glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase from heart and muscle

Proteins: Structure, Function and Genetics

Volumn 63, Issue 3, 2006, Pages 501-511

  Svedružić, Željko M ^a,b   Spivey, H Olin ^a  

^a OKLAHOMA STATE UNIVERSITY   (United States)

^b WASHINGTON STATE UNIVERSITY   (United States)

Author keywords

Excluded volume effect; Metabolic regulation; Metabolon; Molecular crowding; Supramolecular organization

Indexed keywords

AGAROSE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LACTATE DEHYDROGENASE; MACROGOL; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; CRYSTAL STRUCTURE; ELECTROPHORESIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; GLYCOLYSIS; HEART; MAMMAL; MUSCLE TISSUE; PRECIPITATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION;

ANIMALS; BINDING SITES; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; L-LACTATE DEHYDROGENASE; MUSCLE, SKELETAL; MYOCARDIUM; PROTEIN STRUCTURE, TERTIARY; RABBITS; SWINE;

MAMMALIA;

EID: 33646058589     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20862     Document Type: Article

References (74)

1. Srere PA. Protein Crystals as a model for mitochondrial matrix proteins. Trends Biochem Sci 1981;6:4-6.
2. Goodsell DS. Inside a living cell. Trends Biochem Sci 1991;16:203-206.
3. Clegg SJ. Cellular infrastructure and metabolic organization. In: Stadtman ER, Chock PB, editors. From metabolite, to metabolism, to metabolon. Volume 33, current topics in cellular regulation. New York: Academic Press; 1992. p 3-15.
4. Zimmerman SB, Minton AP. Macromoleculare crowding: biochemical, biophysical, and physiological consequences. Annu Rev Biophys Biomol Struct 1993;22:27-65.
5. Srere PA. Enzyme concentrations in tissues. Science 1967;158:936-937.
6. Srere PA. Is there an organization of krebs cycle enzymes in the mitochondrial matrix? In: Mehlman MA, Hanson RW, editors. Energy metabolism and the regulation of metabolic processes in mitochondria. New York: Academic Press; 1972. p 79-91.
7. Berg OG. Influence of macromolecular crowding on thermodynamic activity: solubility and dimerisation constants for spherical and dumbbell-shaped molecules in a hard-sphere mixture. Biopolymers 1990;30:1027-1037.
8. Garner MM, Burg MB. Macromolecular crowding and confinement in cells exposed to hypertonicity. Am J Physiol 1994;266: C877-C892.
9. Minton AP. Implications of macromolecular crowding for protein assembly. Curr Opin Struct Biol 2000;10:34-39.
10. Lerman LS. Physico-chemical properties of the nucleic acids. In: Duchesne J, editor. Physico-chemical properties of the nucleic acids. New York: Academic Press; 1973.
11. Srere PA. Macromolecular interactions: tracing the roots. Trends Biochem Sci 2000;25:150-153.
12. Nooren IM, Thornton JM. Diversity of protein-protein interactions. EMBO J 2003;22:3486-3492.
13. Srere PA, Mathews CK. Purification of multienzyme complexes. Methods Enzymol 1990;182:539-551.
14. Ovadi J. Physiological significance of metabolite channeling. J Theor Biol 1991;152:1-22.
15. Srere PA. Complexes of sequential metabolic enzymes. Annu Rev Biochem 1987;56:89-124.
16. Srere PA. 17th Fritz Lipmann lecture. Wanderings (wonderings) in metabolism. Biol Chem Hoppe Seyler 1993;374:833-842.
17. Sumegi B, McCammon MT, Sherry AD, Keys DA, McAlister-Henn L, Srere PA. Metabolism of [3-13C]pyruvate in TCA cycle mutants of yeast. Biochemistry 1992;31:8720-8725.
18. 13C NMR studies. Biochemistry 1993;32:12725-12729.
19. Kispal G, Evans CT, Malloy C, Srere PA. Metabolic studies on citrate synthase mutants of yeast. A change in phenotype following transformation with an inactive enzyme. J Biol Chem 1989;264:11204-11210.
20. Merz JM, Webster TA, Appleman JR, Manley ER, Yu HA, Datta A, Ackerson BJ, Spivey HO. Polyethylene glycol-induced heteroassociation of malate dehydrogenase and citrate synthase. Arch Biochem Biophys 1987;258:132-142.
21. Halper LA, Srere PA. Interaction between citrate synthase and mitochondrial malate dehydrogenase in the presence of polyethylene glycol. Arch Biochem Biophys 1977;184:529-534.
22. Fahien LA, Kmiotek EH, MacDonald MJ, Fibich B, Mandic M. Regulation of malate dehydrogenase activity by glutamate, citrate, alpha-ketoglutarate, and multienzyme interaction. J Biol Chem 1988;263:10687-10697.
23. Fahien LA, Kmiotek E, Smith L. Glutamate dehydrogenase-malate dehydrogenase complex. Arch Biochem Biophys 1979;192:33-46.
24. Fahien LA, Kmiotek E. Precipitation of complexes between glutamate dehydrogenase and mitochondrial enzymes. J Biol Chem 1979;254:5983-5990.
25. Fahien LA, MacDonald MJ, Teller JK, Fibich B, Fahien CM. Kinetic advantages of hetero-enzyme complexes with glutamate dehydrogenase and the alpha-ketoglutarate dehydrogenase com-plex. J Biol Chem 1989;264:12303-12312.
26. Ashmarina LI, Pshezhetsky AV, Spivey HO, Potier M. Demonstration of enzyme associations by countermigration electrophoresis in agarose gel. Anal Biochem 1994;219:349-355.
27. Datta A, Merz JM, Spivey HO. Substrate channeling of oxalacetate in solid-state complexes of malate dehydrogenase and citrate synthase. J Biol Chem 1985;260:15008-15012.
28. Lindbladh C, Rault M, Hagglund C, Small WC, Mosbach K, Bulow L, Evans C, Srere PA. Preparation and kinetic characterization of a fusion protein of yeast mitochondrial citrate synthase and malate dehydrogenase. Biochemistry 1994;33:11692-11698.
29. Knull HR, Walsh JL. Association of glycolytic enzymes with the cytoskeleton. Curr Top Cell Regul 1992;33:15-30.
30. Walsh JL, Knull HR. Heteromerous interactions among glycolytic enzymes and of glycolytic enzymes with F-actin: effects of poly(ethylene glycol). Biochim Biophys Acta 1988;952:83-91.
31. Walsh JL, Keith TJ, Knull HR. Glycolytic enzyme interactions with tubulin and microtubules. Biochim Biophys Acta 1989;999:64-70.
32. Sirover MA. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta 1999;1432:159-184.
33. Srivastava DK, Bernhard SA. Biophysical chemistry of metabolic reaction sequences in concentrated enzyme solution and in the cell. Annu Rev Biophys Biophys Chem 1987;16:175-204.
34. Nygaard AP, Rutter WJ. Interaction of pyridine-nucleotide linked enzymes. Acta Chem Scand 1956;10:37-48.
35. Cori CF, Velick SF, Cori GT. The combination of diphosphopyridine nucleotide with glyceraldehyde phosphate dehydrogenase. Biochim Biophys Acta 1950;4:160-169.
36. Muronetz VI, Shcherbatova NA, Nagradova NK. Interaction of NAD-dependent dehydrogenases with human erythrocyte membranes. Evidence that D-glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase are catalytically active in a membrane-bound state. Appl Biochem Biotechnol 1996;61:39-46.
37. Campanella ME, Chu H, Low PS. Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane. Proc Natl Acad Sci USA 2005;102:2402-2407.
38. Fukushima T, Decker RV, Anderson WM, Spivey HO. Substrate channeling of NADH and binding of dehydrogenases to complex I. J Biol Chem 1989;264:16483-16488.
39. Grandier-Vazeille X, Bathany K, Chaignepain S, Camougrand N, Manon S, Schmitter JM. Yeast mitochondrial dehydrogenases are associated in a supramolecular complex. Biochemistry 2001;40:9758-9769.
40. Ushiroyama T, Fukushima T, Styre JD, Spivey HO. Substrate channeling of NADH in mitochondrial redox processes. In: Stadtman ER, Chock PB, editors. From metabolite, to metabolism, to metabolon. Volume 33, current topics in cellular regulation. New York: Academic Press; 1992. p 291-307.
41. Srivastava DK, Bernhard SA. Mechanism of transfer of reduced nicotinamide adenine dinucleotide among dehydrogenases. Biochemistry 1985;24:623-628.
42. You KS. Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions. CRC Crit Rev Biochem 1985;17:313-451.
43. Srivastava DK, Smolen P, Betts GF, Fukushima T, Spivey HO, Bernhard SA. The direct transfer of NADH between α-glycerol phosphate dehydrogenase and lactate dehydrogenase. Fact or misinterpretation? Proc Natl Acad Sci USA 1989;86:6464-6468.
44. Wu XM, Gutfreund H, Chock PB. Kinetic method for differentiating mechanisms for ligand exchange reactions: application to test for substrate channeling in glycolysis. Biochemistry 1992;31:2123-2128.
45. Spivey HO. Evidence of NADH channeling between dehydrogenases. J Theor Biol 1991;152:103-107.
46. Wu X, Gutfreund H, Lakatos S, Chock PB. Substrate channeling in glycolysis: a phantom phenomenon. Proc Natl Acad Sci USA 1991;88:497-501.
47. Brooks SP, Storey KB. Re-evaluation of the glycerol-3-phosphate dehydrogenase/L-lactate dehydrogenase enzyme system. Evidence against the direct transfer of NADH between active sites. Biochem J 1991;278(Pt 3):875-881.
48. Keizer J, Smolen P. Mechanisms of metabolite transfer between enzymes: diffusional versus direct transfer. Curr Top Cell Regul 1992;33:391-405.
49. Berry MN, Phillips JW, Grivell AR. Interactions between mitochondria and cytoplasm in isolated hepatocytes. Curr Top Cell Regul 1992;33:309-328.
50. Colowick SP. Separation of proteins by use of adsorbents. Methods Enzymol 1955;1:91-98.
51. Bergmeyer HU, editor. Enzyme assays. Vol. 2. 3rd ed. New York: John Wiley & Sons Inc.; 1986.
52. Schuck P. Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation. Biophys J 1998;75:1503-1512.
53. Honig B, Nicholls A. Classical electrostatics in biology and chemistry. Science 1995;268:1144-1149.
54. Beeckmans S, Kanarek L. 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 1981;117:527-535.
55. Beeckmans S, Van Driessche E, Kanarek L. The visualization by affinity electrophoresis of a specific association between the consecutive citric acid cycle enzymes fumarase and malate dehydrogenase. Eur J Biochem 1989;183:449-454.
56. Cann JR. Theory and practice of gel electrophoresis of interacting macromolecules. Anal Biochem 1996;237:1-16.
57. Miekka SI, Ingham KC. Influence of hetero-association on the precipitation of proteins by poly(ethylene glycol). Arch Biochem Biophys 1980;203:630-641.
58. Ingham KC. Protein precipitation with polyethylene glycol. Methods Enzymol 1984;104:351-356.
59. Philo J. Meassuring sedimentation, diffusion, and molecular weights of small molecules by direct fitting of sedimentation velocity concentration profiles. In: Schuster T, Laue T, editors. Modern analytical ultracentrifugation. Boston: Basel; Berlin: Birkhauser; 1994. p 350.
60. Hoskins AA, Anand R, Ealick SE, Stubbe J. The formylglycinamide ribonucleotide amidotransferase complex from Bacillus subtilis: metabolite-mediated complex formation. Biochemistry 2004;43:10314-10327.
61. Scheek RM, Slater EC. Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle. Methods Enzymol 1982;89(Pt D):305-309.
62. Holbrook JJ, Liljas S, Steindel SJ, Rossman MG, editors. Lactate dehydrogenase. 3rd ed. Vol. XI. New York: Academic Press; 1975.
63. Harris JI, Waters M, editors. Glyceraldehyde-3-phosphate dehydrogenase. 3rd ed. Vol. XIII. New York: Academic Press; 1976.
64. Velot C, Mixon MB, Teige M, Srere PA. Model of a quinary structure between Krebs TCA cycle enzymes: a model for the metabolon. Biochemistry 1997;36:14271-14276.
65. Cowan-Jacob SW, Kaufmann M, Anselmo AN, Stark W, Grutter MG. Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase. Acta Crystallogr D Biol Crystallogr 2003;59:2218-2227.
66. Grau UM, Trommer WE, Rossmann MG. Structure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7 A resolution. J Mol Biol 1981;151:289-307.
67. Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL. Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins 2001;43:175-185.
68. Newsholme EA, Leech AR. Biochemistry for medical students. New York: Wiley; 1985.
69. Newsholme EA, Board M. Application of metabolic-control logic to fuel utilization and its significance in tumor cells. Adv Enzyme Regul 1991;31:225-246.
70. Pearson WR, Wood T, Zhang Z, Miller W. Comparison of DNA sequences with protein sequences. Genomics 1997;46:24-36.
71. Rossman MG, Liljas A, Branden C-I, Banaszak LJ. Evolutionary and structural relationships among dehydrogenase. In: Boyer PD, editor. The enzymes. 3rd ed. Vol. XI. New York: Academic Press; 1975. p 61-102.
72. Lehoux EA, Baker SM, Kovina MV, Hays FA, Spivey HO. Absence of evidence for metabolite-modulated association between alpha-glycerol-3-phosphate dehydrogenase and L-lactate dehydrogenase. Biochemistry 2003;42:6259-6263.
73. Dunn CR, Wilks HM, Halsall DJ, Atkinson T, Clarke AR, Muirhead H, Holbrook JJ. Design and synthesis of new enzymes based on the lactate dehydrogenase framework. Philos Trans R Soc Lond B Biol Sci 1991;332:177-184.
74. Mercer WD, Winn SI, Watson HC. Twinning in crystals of human skeletal muscle D-glyceraldehyde-3- phosphate dehydrogenase. J Mol Biol 1976;104:277-283.