Enzymes and the supramolecular organization of the living cell. Information transfer within supramolecular edifices and imprinting effects

Cellular and Molecular Life Sciences

Volumn 54, Issue 11, 1998, Pages 1231-1248

  Ricard, J ^a   Gontero, B ^a   Avilan, L ^a   Lebreton, S ^a  

^a UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

Imprinting effects in proteins; Information transfer; Multienzyme complexes

Indexed keywords

GLYCERALDEHYDE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; PHOSPHORIBULOKINASE;

CATALYSIS; CELL ACTIVITY; CHLAMYDOMONAS; CHLOROPLAST; COMPLEX FORMATION; ENZYME ACTIVITY; MEMBRANE BINDING; MOLECULAR DYNAMICS; PROTEIN INTERACTION; REVIEW; THERMODYNAMICS;

EID: 0031794306     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050250     Document Type: Review

References (134)

1. Goodsell D. S. (1991) Inside a living cell. Trends Biochem. Sci. 16: 203-206
2. Srere P. A. (1980) The infrastructure of the mitochondrial matrix. Trends Biochem. Sci. 5: 120-121
3. Zimmerman S. B. and Trach S. O. (1991) Estimation of macromolecular concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J. Mol. Biol. 222: 599-622
4. Srivastava D. K. and Bernhard S. A. (1986) Metabolite transfer via enzyme-enzyme complexes. Science 234: 1081-1086
5. Srere P. A. (1987) Complexes of sequential metabolic enzymes. Annu. Rev. Biochem. 56: 89-124
6. Easterby J. S. (1989) The analysis of metabolite channelling in multienzyme complexes and multifunctional proteins. Biochem. J. 264: 605-607
7. Srere P. A. and Ovadi J. (1990) Enzyme-enzyme interactions and their metabolic role. FEBS Lett. 268: 360-368
8. Ovadi J. (1991) Physiological significance of metabolic channeling. J. Theor. Biol. 152: 1-22
9. Wu X., Gutfreund H., Lakatos S. and Chock P. B. (1991) Substrate channelling in glycolysis: a phantom phenomenon. Proc. Natl. Acad. Sci. USA 88: 497-501
10. Petersson G. (1991) No convincing evidence is available for metabolite channelling between enzymes forming dynamic complexes. J. Theor. Biol. 152: 65-69
11. Sainis J. K. and Jawali N. (1994) Channeling of the intermediates and catalytic falicitation to Rubisco in a multienzyme complex of Calvin cycle enzymes. Ind. J. Biochem. Biophys. 31: 215-220
12. Mendes P., Kell D. B. and Westerhoff H. V. (1996) Why and when channelling can decrease pool size at constant net flux in a simple dynamic channel. Biochim. Biophys. Acta 1289: 175-186
13. Pan P., Woehl E. and Dunn M. F. (1997) Protein architecture, dynamics and allostery in tryptophan synthase channeling. Trends Biochem. Sci. 22: 22-27
14. Deutscher M. P. (1984) The eucaryotic aminoacyl-tRNA synthetase complex: suggestions for its structure and function. J. Biol. Cell 99: 373-377
15. Mirande M., Lazard M., Martinez R. and Latreille M.-T. (1992) Engineering mammalian aspartyl-tRNA synthetase to probe structural features mediating its association with the multisynthetase complex. Eur. J. Biochem. 203: 459-466
16. Kerjan P., Cerini C., Semeriva M. and Mirande M. (1994) The multienzyme complex containing nine aminoacyl-tRNA synthetases is ubiquitous from Drosophila to mammals. Biochim. Biophys. Acta 1199: 293-297
17. Harris C. L. and Kolanko C. J. (1995) Aminoacyl-tRNA synthetase complex in Saccharomyces cerevisiae. Biochem. J. 309: 321-324
18. Castellan G. W. (1971) Physical Chemistry, 2nd ed., Addison-Wesley, Reading, MA
19. Haken H. (1978) Synergetics, 2nd ed., Springer, Berlin
20. Margenau H. and Murphy C. M. (1956) The Mathematics of Physics and Chemistry, Van Nostrand, Princeton
21. Anfinsen C. B., Haber E., Sela M. and White F. H. (1961) The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain. Proc. Natl. Acad. Sci. USA 47: 1309-1314
22. Anfinsen C. B. (1973) Principles that govern the folding of protein chains. Science 181: 223-230
23. Anfinsen C. B. and Sheraga M. A. (1975) Experimental and theoretical aspects of protein folding. Adv. Prot. Chem. 29: 205-300
24. Creighton T. E. (1983) Proteins, Freeman, New York
25. Yon J. M. (1997) Protein folding: concepts and perspectives. Cell. Mol. Life Sci. 53: 557-567
26. Levinthal C. (1968) Are there pathways for protein folding? J. Chem. Phys. 65: 44-45
27. Wetlaufer D. B. (1973) Nucleation, rapid folding and globular intrachain regions in proteins. Proc. Natl. Acad. Sci. USA 70: 697-701
28. Deshaies R. J., Koch B. D., Werner-Washburne M., Craig E. A. and Schekman R. (1988) A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332: 800-805
29. Chirico W. J., Waters M. G. and Blobel G. (1988) 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 332: 805-810
30. Ellis R. J. (1991) Molecular chaperones. Annu. Rev. Biochem. 60: 321-347
31. Langer T. and Neupert W. (1996) Chaperonin-mediated folding and assembly of proteins in mitochondria. In: The Chaperonins, pp. 91-106, Ellis R. J. (ed.), Academic Press, San Diego
32. Ellis R. J. and Hemmingsen S. M. (1989) Molecular diaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem. Sci. 14: 339-342
33. Martin J., Langer T., Boteva R., Schramel A., Horwich A. L. and Harlt F. U. (1991) Chaperonin-mediated protein folding at the surface of GroEL through a 'molten globule' like intermediate. Nature 352: 36-42
34. Pelham H. R. B. (1986) Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 46: 959-961
35. Nguyen V. T., Morange M. and Bensaude O. (1989) Protein denaturation during heat shock and related stress. Escherichia coli beta-galactosidase and Photinus pyralis luciferase inactivation in mouse cells. J. Biol. Chem. 264: 10487-10492
36. Pinto M., Morange M. and Bensaude O. (1991) Denaturation of proteins during heat shock. In vivo recovery of solubility and activity of reporter enzymes. J. Biol. Chem. 266: 13941-13946
37. Ellis R. J. (1996) The Chaperonins, Academic Press, San Diego
38. Goldberg M. E. (1973) L'étal natif est-il l'état fondamental? In: Dynamic Aspects of Conformation Changes in Biological Macromolecules,pp. 57-65. Sadron C. (ed.), Reidel, Dordrecht
39. Ikemura H., Takagi H. and Inouye M. (1988) Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli. Biol. Chem. 262: 7859-7864
40. Shinde U., Li Y., Chatterjee S. and Inouye M. (1993) Folding pathway mediated by an intramolecular chaperone. Proc. Natl. Acad. Sci. USA 90: 6924-6928
41. Zhu X. L., Ohta Y., Jordan F. and Inouye M. (1989) Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in intermolecular process. Nature 339: 483-484
42. Eder J., Rheinnecker M. and Fersht A. R. (1993) Folding of subtilisin BPN: role of the pro-sequence. J. Mol. Biol. 233: 293-304
43. Strausberg S., Alexander P., Wang L., Schwarz F. and Bryan P. (1993) Catalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN interactions with its propeptide fragment. Biochem. 32: 8312-8319
44. Shinde U. P., Liu J. J. and Inouye M. (1997) Protein memory through altered folding mediate by intramolecular chaperones. Nature 389: 520-522
45. Silen J. L. and Agard D. A. (1989) The alplia-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo. Nature 341: 462-464
46. 2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence in Escherichia coli. FEMS Microbiol. Lett. 71: 73-77
47. Winther J. R., Sorensen P. and Kielland-Grandt M. C. (1994) Refolding of carboxypeptidase Y folding intermediate in vitro by low affinity binding of the pro-region. J. Biol. Chem. 268: 22007-22013
48. Eder J., Rheinnecker M. and Fersht A. R. (1993) Folding of subtilisin BPN: characterization of a folding intermediate. Biochem. 32: 18-26
49. Shinde U. P. and Inouye M. (1995) Folding pathway mediated by an intramolecular chaperone: characterization of the structural changes in pro-subtilisin E coincident with autoprocessing. J. Mol. Biol. 252: 25-30
50. Baker D., Sohl Y. and Agard D. A. (1992) A protein-folding reaction under kinetic control. Nature 356: 263-265
51. Eder J. and Fersht A. R. (1995) Pro-sequence-assisted protein folding. Mol. Microbiol. 16: 609-614
52. Prusiner S. B. (1989) Scrapie prions. Annu. Rev. Microbiol. 43: 345-374
53. Prusiner S. B. (1991) Molecular biology of prion diseases. Science 252: 1515-1522
54. Prusiner S. B. (1997) Prion diseases and the BSE crisis. Science 278: 245-251
55. Bolton D. C., McKinley M. P. and Prusiner S. B. (1982) Identification of a protein that purifies with the scrapie prion. Science 218: 1309-1311
56. Gabizon R., McKinley M. P., Groth D. and Prusiner S. B. (1988) Immunoaffinity purification and neutralization of scrapie prion infectivity. Proc. Natl. Acad. Sci. USA 85: 6617-6622
57. McClintock D. K. and Bell P. M. (1971) The mechanism of activation of human plasminogen by streptokinase. Biochem. Biophys. Res. Commun. 43: 694-702
58. Reddy K. N. and Markus G. (1972) Mechanism of activation of human plasminogen by streptokinase. Presence of active center in streptokinase-plasminogen complex. J. Biol. Chem. 247: 1683-1691
59. Schick L. A. and Castellino F. Y. (1973) Interaction of streptokinase and rabbit plasminogen. Biochem. 12: 4315-4321
60. Summaria L., Wohl R. C., Boreisha I. G. and Robbins K. C. (1982) A virgin enzyme derived from human plasminogen. Specific cleavage of the arginyl-560-valyl peptide bond in the diisopropoxyphosphinyl virgin enzyme by plasminogen activators. Biochem. 21: 2056-2059
61. Buck F. F., Hummel B. C. N. and De Renzo E. C. (1968) Interaction of streptokinase and human plasminogen V. Studies on the nature and mechanism of formation of the enzymatic site of the activator complex. J. Biol. Chem. 243: 3648-3654
62. Groskopf W. R., Summaria L. and Robbins K. C. (1969) Studies on the active center of human plasmin. The serine and histidine residues. J. Biol. Chem. 244: 359-365
63. Reed G. L., Lin L. F., Parkami-Seren B. and Kussie P. (1995) Identification of a plasminogen binding region in streptokinase that is necessary for the creation of a functional streptokinase-plasminogen activation complex. Biochem. 34: 10266-10271
64. 2-fixing enzyme complex in spinach chloroplasts. Z. Naturforseh. 27b: 925-932
65. Gontero B., Cardenas M. L. and Ricard J. (1988) A functional five enzyme complex of chloroplasts involved in the Calvin cycle. Eur J. Biochem. 173: 437-446
66. Ricard J., Giudici-Orticoni M. T. and Gontero B. (1994) The modulation of enzyme reaction rates within multi-enzyme complexes. I. Statistical thermodynamics of information transfer through multi-enzyme complexes. Eur. J. Biochem. 226: 993-998
67. Gontero B., Giudici-Orticoni M. T. and Ricard J. (1994) The modulation of enzyme reaction rates within multi-enzyme complexes. 2. Information transfer within a chloroplast multi-enzyme complex containing ribulose bisphosphate carboxylase-oxygenase. Eur. J. Biochem. 226: 999-1006
68. Rault M., Giudici-Orticoni M. T., Gontero B. and Ricard J. (1993) Structural and functional properties of a multi-enzyme complex of spinach chloroplasts. I. Stoichiometry of the polypeptide chains. Eur. J. Biochem. 217: 1065-1073
69. Gontero B., Mulliert G., Rault M., Giudici-Orticoni M. T. and Ricard J. (1993) Structural and functional properties of a multi-enzyme complex of spinach chloroplasts. 2. Modulation of the kinetic properties of enzymes in the aggregated state. Eur. J. Biochem. 217: 1075-1082
70. Avilan L., Gontero B., Lebreton S. and Ricard J. (1997) Memory and imprinting effects in multi-enzyme complexes. I. Isolation, dissociation and reassociation of a phosphoribulokinase-glyceraldehyde-3-phosphate dehydrogenase complex from Chlamydomonas reinhardtii chloroplasts. Eur. J. Biochem. 246: 78-84
71. Lebreton S., Gontero B., Avilan L. and Ricard J. (1997) Memory and imprinting effects in multienzyme complexes. II. Kinetics of the bi-enzyme complex from Chlamydomonas reinhardtii and hysteretic activation of chloroplast oxidized phosphoribulokinase. Eur. J. Biochem. 246: 85-91
72. Avilan L., Gontero B., Lebreton S. and Ricard J. (1997) Information transfer in multienzyme complexes. II. The role of Arg64 of Chlamydomonas reinhardtii phosphoribulokinase in the information transfer between glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase. Eur. J. Biochem. 250: 296-302
73. Lebreton S., Gontero B., Avilan L. and Ricard J. (1997) Information transfer in multienzyme complexes. I. Thermodynamics of conformational constraints and memory effects in the bienzyme glyceraldehyde-3-phosphate dehydrogenase-phosphoribulokinase complex of Chlamydomonas reinhardtii chloroplasts. Eur. J. Biochem. 250: 286-295
74. Nicholson S., Easterby J. S. and Powls R. (1987) Properties of a multimeric protein complex from chloroplasts possessing potential activities of NADPH-dependent glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase. Eur. J. Biochem. 162: 423-431
75. Clasper S., Easterby J. S. and Powls R. (1991) Properties of two high-molecular mass forms of GraPDH from spinach leaf, one of which also possesses latent phosphoribulokinase activity. Eur. J. Biochem. 202: 1239-1246
76. Süss K. H., Arkona C., Manteuffel R., and Adler K. (1993). Calvin cycle multienzyme complexes are bound to chloroplast thylakoid membranes of higher plants in situ. Proc. Natl. Acad. Sci. USA 90: 5514-5518
77. + reductase, and nitrite reductase with thylakoid and pyrenoid membranes of Chlamydomonas reinhardtii chloroplasts as revealed by immunoelectron microscopy. Plant Physiol. 107: 1387-1397
78. Sainis J. K. and Harris C. G. (1986) The association of ribulose-1,5-bisphosphate carboxylase-oxygenase, with phosphoribulokinase and phosphoribose isomerase. Biochem. Biophys. Res. Commun. 139: 947-954
79. Sainis J. K., Merriam K. and Harris G. (1989) The association of D-ribulose-1,5-bisphosphate carboxylase oxygenase with phosphoribulokinase. Plant Physiol. 89: 368-374
80. Hosur M. V., Sainis J. K. and kannan K. K. (1993) Crystallization and X-ray analysis of a multienzyme complex containing RUBISCO and Ru5P. J. Mol. Biol. 234: 1274-1278
81. Anderson L. E., Goldhaber-Gordon I. M., Li D., Tang X., Xiang M. and Prakash N. (1995) Enzyme-enzyme interaction in the chloroplast: glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase. Planta 196: 245-255
82. Bourne H. R., Sanders D. A. and McCormick F. (1990) The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348: 125-132
83. Bourne H. R., Sanders D. A. and McCormick F. (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature 349: 117-127
84. Lowy D. R. and Willumsen B. M. (1993) Function and regulation of RAS. Annu. Rev. Biochem. 62: 851-891
85. Gideon P., John J., Frech M., Lautwein A., Clark R., Scheffler J. E. et al. (1992) Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity. Mol. Cell. Biol. 12: 2050-2056
86. Eccleston J. F., Moore K. J. M., Morgan L., Skinner R. H. and Lowe P. N. (1993) Kinetics of interaction between normal and proline 12 Ras and the GTPase-activating proteins. p120-GAP and neurofibromin. J. Biol. Chem. 268: 27012-27019
87. NRAS, the NRAS protooncogene product, is accompanied by a conformational change in the wild-type protein: use of a single fluorescent probe at the catalytic site. Proc. Natl. Acad. Sci. USA 87: 3562-3565
88. Rensland H., Lautwein A., Wittinghofer A. and Goody R. S. (1991) Is there a rate-limiting step before GTP cleavage by H-ras p21? Biochemistry 36: 11181-11185
89. ras and other GTP-binding proteins. Nature Struct. Biol. 2: 36-44
90. Wittinghofer A., Scheffzek K. and Ahmadian M. R. (1997) The interaction of Ras with GTPase-activating proteins. FEBS Lett. 410: 63-67
91. Ahmadian M. R., Hoffmann U., Goody R. S. and Wittinghofer A. (1997) Individual rate constants for the interaction of Ras proteins with GTPase-activating proteins determined by fluorescence spectroscopy. Biochemistry 36: 4535-4541
92. Ahmadian M. R., Stege P., Scheffezek K. and Wittinghofer A. (1997) Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras. Nature Struct. Biol. 4: 686-689
93. Bourne H. R. (1997) The arginine finger strikes again. Nature 389: 673-674
94. Sheffzek K., Lautwein A., Kabsch W., Ahmadian M. R. and Wittinghofer A. (1996) Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras. Nature 384: 591-596
95. Newton A. C. (1995) Seeing two domains. Curr. Biol. 5: 973-976
96. House C. and Kemp B. E. (1987) Protein kinase C contains a pseudo prototope in its regulatory domain. Science 238: 1726-1728
97. Bell R. M. and Burns D. J. (1991) Lipid activation of protein kinase C. J. Biol. Chem. 266: 4661-4664
98. Borner C., Filipuzzi I., Wartmann M., Eppenberger U. and Fabbro D. (1989) Biosynthesis and posttranslational modifications of protein kinase C in human breast cancer cells. J. Biol. Chem. 264: 13902-13909
99. Dutil E. M., Keranen L. M., DePaoli-Roach A. A. and Newton A. C. (1994) In vivo regulation of protein kinase C by transphosphorylation followed by autophosphorylation. J. Biol. Chem. 269: 29359-29362
100. Cazaubon S., Bornancin F. and Parker P. J. (1994) Threonine-497 is a critical site for permissive activation of protein kinase C alpha. Biochem. J. 301: 443-448
101. Orr J. W. and Newton A. C. (1994) Requirement for negative charge on 'activation loop' of protein kinase C. J. Biol. Chem. 269: 27715-27718
102. Orr J. W. and Newton A. C. (1994) Intrapeptide regulation of protein kinase C. J. Biol. Chem. 269: 8383-8387
103. Orr J. W., Keranen L. M. and Newton A. C. (1992) Reversible exposure of the pseudosubstrate domain of protein kinase C by phosphatidylserine and diacylglycerol. J. Biol. Chem. 267: 15263-15266
104. Takai Y., Kishimoto A., Iwaso Y., Kawahara Y., Mori T. and Nishizyka Y. (1979) Calcium-dependent activation of a multi-functional protein kinase by membrane phospholipids. J. Biol. Chem. 254: 3692-3695
105. Newton A. C. (1995) Protein kinase C: structure, function and regulation. J. Biol. Chem. 270: 28495-28498
106. Sarda L. and Desnuelle P. (1958) Action de la lipase pancréatique sur les esters en émulsion. Biochim. Biophys. Acta 30: 513-521
107. Desnuelle P., Sarda L. and Ailhaud G. (1960) Inhibition de la lipase pancréatique par le diéthyl-p-nitrophénylphosphate. Biochim. Biophys. Acta 37: 570-571
108. Borgström B. and Bruckman M. L. (1984) Lipases, Elsevier, Amsterdam
109. Cygler M. and Schrag J. D. (1997) Structure as basis for understanding interfacial properties of lipases. Methods Enzymol. 284: 3-27
110. Ferrato F., Carriere F., Sarda L. and Verger R. (1997) A critical reevaluation of the phenomenon of interfacial activation. Methods Enzymol. 286: 327-347
111. Brady L., Brzozowski A. M., Derewenda Z. S., Dodson E., Dodson G., Tolley S. et al. (1990) A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 343: 767-770
112. Winkler F. K., D'Arcy A. and Hunziker W. (1990) Structure of human pancreatic lipase. Nature 343: 771-774
113. Schrag J. D., Li Y. G., Wu S. and Cygler M. (1991) Ser-his-glu triad forms the catalytic site of the lipase from Geotrichum candidum. Nature 351: 761-764
114. Blow D. M. (1990) Enzymology: more of the catalytic triad. Nature 343: 694-695
115. Van Tilbeurgh H., Egloff M. P., Martinez C., Rugani N., Verger P. and Cambillau C. (1993) Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature 362: 814-820
116. Brzozowski A. M., Derewenda U. D., Derewenda Z. S., Dodson G. G., Lawson D. M., Turkenburg J. P. et al. (1991) A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 351: 491-494
117. Derewenda U., Brzozowski A. M., Lawson D. M. and Derewenda U. D. (1992) Catalysis at the interface: the anatomy of a conformational change in triglyceride lipase. Biochemistry 31: 1532-1541
118. Srere P. A. (1994) Complexities of metabolic regulation. Trends Biochem. Sci. 19: 519-520
119. Vlatakis G., Andersson L. I., Muller R. and Mosbach K. (1993) Drug assay using antibody mimics made by molecular imprinting. Nature 361: 645-647
120. Russell A. J. and Klibanov A. M. (1988) Inhibition induced enzyme activation in organic solvents. J. Biol. Chem. 263: 11624-11626
121. Klibanov A. M. (1995) Enzyme memory: what is remembered and why? Nature 374: 596
122. Yenanawar M. P., Yennawar N. M. and Farber G. K. (1995) A structural explanation for enzyme memory in nonaqueous solvents. J. Am. Chem. Soc. 117: 577-585
123. Dabulis K. and Klibanov A. M. (1993) Dramatic enhancement of enzymatic activity in organic solvents by lyoprotectans. Biotechnol. Bioeng. 41: 566-571
124. Khmelnitsky Y., Welch S. H., Clark D. S. and Dordick J. S. (1994) Salts dramatically enhance activity of enzymes suspended in organic solvents. J. Am. Chem. Soc. 116: 2647-2648
125. Ricard J., Meunier J. C. and Buc J. (1974) Regulatory behavior of monomeric enzymes. 1. The mnemonical enzyme concept. Eur. J. Biochem. 49: 195-208
126. Meunier J. C., Buc J., Navarro A. and Ricard J. (1974) Regulatory behavior of mionomeric enzymes. 2. A wheat-germ hexokinase as a mnemonical enzyme. Eur. J. Biochem. 49: 209-223
127. Ricard J., Buc J. and Meunier J. C. (1977) Enzyme memory. 1. A transient kinetic study of wheat-germ hexokinase LI. Eur. J. Biochem. 80: 581-592
128. Buc J., Ricard J. and Meunier J. C. (1977) Enzyme memory. 2. Kinetics and thermodynamics of the slow conformation changes of wheat-germ hexokinase LI. Eur. J. Biochem. 80: 593-601
129. Meunier J. C., Buc J. and Ricard J. (1979) Enzyme memory. Effect of glucose 6-phosphate and temperature on the molecular transition of wheat-germ hexokinase LI. Eur. J. Biochem. 97: 573-583
130. Soulie J. M., Riviere M. and Ricard J. (1988) Enzymes as biosensors. 2. Hysteretic response of chloroplastic fructose-1,6-bisphosphatase to fructose-2,6-bisphosphate. Eur. J. Biochem. 176: 111-117
131. Storer A. C. and Cornish-Bowden A. (1976) Kinetics of rat liver glucokinase. Co-operative interactions with glucose at physiologically significant concentrations. Biochem. J. 159: 7-14
132. Neet K. E. and Ainslie G. R. (1980) Hysteretic enzymes. Methods Enzymol. 64: 192-226
133. Neet K. E. (1995) Cooperatively in enzyme function: equilibrium and kinetic aspects. Methods Enzymol. 249: 519-567
134. Kuhn T. S. (1967) The Structure of Scientific Revolutions. University of Chicago Press, Chicago