Τόμος 3 (1989) – Τεύχος 2 – Άρθρο 1 – Επιθεώρηση Κλινικής Φαρμακολογίας και Φαρμακοκινητικής-Διεθνής Έκδοση – Volume 3 (1989) – Issue 2 – Article 1 – Epitheorese Klinikes Farmakologias και Farmakokinetikes-International Edition

Title X-ray diffraction studies on enzyme catalysis and allosteric control of glycogen phosphorylase b
Authors Nikos G. Oikonomakos¹, K. Ravi Acharya², Louise N. Johnson², Anastassios C. Papageorgiou¹ and Demetrios D. Leonidas¹

1.  The National Hellenic Research Foundation, 48 Vas. Constantinou Avenue, Athens 116 35, Greece.

2. Laboratory of Molecular Biophysics, University of Oxford, Oxford 0X1 3QU, U.K.

Citation Oikonomakos, N.G., Acharya, K.R., Johnson, L.N., Papageorgiou, A.C., Leonidas, D.D.: X-ray diffraction studies on enzyme catalysis and allosteric control of glycogen phosphorylase b, Epitheorese Klin. Farmakol. Farmakokinet. 3(2): 69-94 (1989)
Publication Date 1989-10
Full Text Language English
Order – Buy Ηλεκτρονική Μορφή: pdf (10 €)Digital Type: pdf (10 €)

pharmakonpress[at]pharmakonpress[.]gr

Keywords X-ray, diffraction techniques, protein, enzyme, catalysis, allosteric, control, glycogen, phosphorylase b.
Other Terms review article
Summary A brief discussion of some of the basic rules governing the application of X-ray diffraction techniques to the determination of the three-dimensional structure of protein (enzyme) crystals is presented in this report, followed by a description of the current state of our knowledge of the catalytic and structural properties of glycogen phosphorylase, an allosteric enzyme which plays an important role in the control of glycogen metabolism, and the progress that has been made by the most recent results of the crystallographic studies on this enzyme.
References 1.         Phillips, D.C.: The hen egg-white lysozyme molecule. Proc. Natl. Acad Scl. USA 57:484 (1967)

2.         Blake, C.C.F., Mair, G.A., North, A.C.T., Phillips, D.C., and Sarma, V.R.: On the conformation of the hen egg-white lysozyme molecule. Proc. R. Soc. Lond. (Biol.) B167: 365 (1967)

3.         Blake, C.C.F., Johnson, LN., Mair, G.A., North, A.C.T., Phillips, D.C. and Sarma, V.R.: Crystallographic studies of the activity of hen egg-white lysozyme. Proc. R. Soc. Lond. (Biol.) 8167: 378 (1967)

4.         Goodford, P.J.: Drug design by the method of receptor fit. J. Med. Chem. 27: 557 (1984)

5.         Hoi, W.G.J.: Protein crystallography and computer graphics toward rational drug design. Angew. Chem. Int. Ed. Engl. 25: 767 (1986)

6.         Herzberg, O. and Moult, J.: Bacterial resistance to β- lactam antibiotics: crystal structure of β-lactamase from Staphylococcus aureus PCI at 2.5 A resolution. Science 236: 694 (1987)

7.         Wierenga, R.K., Kalk, K.H. and Hoi, W.G.J.: Structure determination of the giycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 A resolution. J. Mot. Biol. 198: 109 (1987)

8.         Shaw, W.V.: The design, synthesis and characterization of factitious proteins. Biochem. J. 246: 1 (1987)

9.         Andersson, I., Knight, S., Schneider, G., Lindqvist, Y„ Lundqvist, T., Branden, C.-I. and Lorimer. G.H.: Crystal structure of the active site of ribulose-biphosphate carboxylase. Nature 337: 229 (1989)

10.       Gerlt, J.A.: Relationships between enzymatic catalysis and active site structure revealed by applications of site-directed mutagenesis. Chem. Rev. 87: 1079 (1987)

11.       Russell,-A.J. and Fersht, A.R.: Rational modification of enzyme catalysis by engineering surface charge. Nature 328: 496 (1987)

12.       Matsumura, M., Becktel, W.J. and Matthews, B.W.: Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of lie 3. Nature 334: 406 (1988)

13.       Upson, H. and Cochran, W.: The determination of crystal structures (rev. ed.), Cornell University Press, Ithaca N.Y., 1966

14.       Stout, G.H. and Jensen, L.H.: X-ray Structure Determination, MacMillan, New York, 1968

15.       Glusker, J.P. and Truebiood, K.N.: Crystal Structure Analysis: A Primer, Oxford University Press, London, 1972

16.       Piundell, T.L. and Johnson, LN.: Protein Crystallography, Academic Press, New York, 1976

17.       Johnson, L.N.: Protein crystallography. In: Modern Methods in Biochemistry, Part A, (Neuberger/Van Deenen, eds), p. 347, 1985

18.       Stuart, D.I.: Protein crystallography. In: Signal Transduction and Protein Phosphorylation (L.M.G. Heilmeyer, ed.), Series A: Life Sciences, vol. 135, p. 45, Plenum Press, New York and London, 1987

19.       Bragg. W.L and Perutz, M.F.: The structure of haemoglobin. VI. Fourier projections on the 010 plane. Proc. Roy. Soc. A225: 315 (1954)

20.       Kendrew, J.C., Bodo, G.r Dintzis, H.M., Parrish, R.G., Wyckoff, H. and Phillips, D.C.: A three dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 181: 662 (1958)

21.       McPherson, A. Jr.: Crystallization of proteins from polyethylene glycol. J. Biol. Chem. 251: 6300 (1976)

22.       McPherson, A.: Preparation and analysis of protein crystals, John Wiley and Sons, New York, Chichester, Brisbane, Toronto, Singapore, 1982

23.       Michel, H.: Crystallization of membrane proteins. Trends Biochem. Sci. 8: 56 (1983)

24.       Giege, R„ Ducruix, A., Fontecilla-Camps, J.A., Feigelson, R. Kern and A. McPherson (eds): Proceedings of the 2nd International Conference on the Crystal Growth of Biological Macromolecules, Bischenberg 1987, a special issue of J. Crystal Growth 90: 1 (1988)

25.       Kasvinsky, P.J. and Madsen, N.B.: Activity of glycogen phosphorylase in the crystalline state. J. Biol. Chem. 251: 6852 (1976)

26.       Fersht, A.: Enzyme Structure and Mechanism, 2nd ed. W.H. Freeman, New York, 1985

27.       Hajdu, J., Acharya, K.R., Stuart, D.I., Barford, D. and Johnson, L.N.: Catalysis in enzyme crystals. Trends Biochem. Sci. 13: 104 (1988)

28.       Cori, C.F. and Cori, G.T.: Mechanism of formation of hexosemonophosphate in muscle and isolation of a new phosphate ester. Proc. Soc. Exp. Biol. Med. 34: 702 (1936)

29.       Monod, J., Changeux, J.-P. and Jacob, F.: Allosteric proteins and cellular control systems. J. Mot Biol. 6: 306 (1963)

30.       Krebs, E.G. and Fishcer, E.H.: The phosphorylase b to a converting enzyme of rabbit skeletal muscle. Biochim. Biophys. Acta 20: 150 (1956)

31.       Fischer, E.H., Graves, D.J., Crittenden, E.R.S. and Krebs, E.G.: Structure of the site phosphorylated in the phosphorylase b to a reaction. J. Biol. Chem. 234: 1698 (1959)

32.       Cohen, P.: Control of Enzyme Activity. 2nd ed., Chapman and Hall, London, 1983

33.       Baranowski, T., Illingworth, B„ Brown, O.H. and Cori, C.F.: The isolation of pyridoxal 5′-phosphate from crystalline muscle phosphorylase. Biochim. Biophys. Acta 25: 16 (1957)

34.       Klein, H.W., Im, M.J. and Palm, D.: Mechanism of the phosphorylase reaction. Utilization of D-gluco-hept-1-enitol in the absence of primer. Eur. J. Biochem. 157: 107 (1986)

35.       Madsen, N.B. and Withers, S.G.: Glycogen phosphorylase. In: Coenzymes and Cofactors, Vol. I, Vitamin B6 Pyridoxal Phosphate (D. Dolphin, R. Poulson and O. Avramovic, eds), p. 355, John Wiley-New York, 1986

36.       Fukui, T. and Tagaya, M.: A novel coenzymatic function of pyridoxal 5′-phosphate. Bio Essays 5: 21 (1986)

37.       Hajdu, J., Acharya, K.R., Stuart, D.I., McLaughlin, P.J., Barford, D., Oikonomakos, N.G., Klein, H. and Johnson, L.N.: Catalysis in the crystal: synchrotron radiation studies with glycogen phosphorylase b. EMBO J. 6: 539 (1987)

38.       Graves, D.J. and Wang, J.H.: α-Glucan phosphorylases-chemical and physical basis of catalysis and regulation. In: The Enzymes (P.D. Boyer, ed.), 3rd ed. Vol. 7, p. 435, Academic Press, New York, 1972

39.       Fleterick, R.J. and Madsen, N.B.: The structures and related functions of phosphorylase a. Annu. Rev. Biochem. 49: 31 (1980)

40.       Helmreich, E.J.M. and Klein, H.W.: The role of pyridoxal phosphate in the catalysis of glycogen phosphorylases. Angew. Chem. int. Ed. Eng. 19: 441 (1980)

41.       Dombradi, V.: Structural aspects of the catalytic and regulatory function of glycogen phosphorylase. Int. J. Biochem. 13: 125 (1981)

42.       Fletterick, R.J. and Sprang, S.R.: Glycogen phosphorylase structures and function. Acc. Chem. Res. 15: 361 (1982)

43.       Madsen, N.B.: Glycogen phosphorylase. In: The Enzymes (P.D. Boyer, E.G. Krebs, eds), 3rd ed. Vol. 17, p. 366, Academic Press, New York, 1986

44.       Johnson, L.N., Hajdu, J., Acharya, K.R., Stuart, D.I., McLaughlin, P.J., Oikonomakos, N.G. and Barford, D.: Glycogen phosphorylase b. In: Allosteric Enzymes (G. Herve, ed.), p. 81, CRC Press, Boca Raton, Florida, 1989

45.       Madsen, N.B.: Glycogen phosphorylase and glycogen synthetase. In: A Study of Enzymes, (S.A. Kuby, ed.). Vol. Ill, Boca Raton, in the press, 1989

46.       Cohen, P.: The role of cyclic-AMP dependent protein kinase in the regulation of glycogen metabolism in mammalian skeletal muscle. Curr. Top. Cell. Reg. 14: 117 (1978)

47.       Hers, H.G.: The control of glycogen metabolism in the liver. Annu. Rev. Biochem. 45: 167 (1976)

48.       Engers, H.D., Bridger, W.A. and Madsen, N.B.: Kinetic mechanism of phosphorylase b. J. Biol. Chem. 244: 5936 (1969)

49.       Engers, H.D., Shechosky, S. and Madsen, N.B.: Kinetic – mechanism of phosphorylase a. I. Initial velocity studies Can. J. Biochem. 48: 746 (1970)

50.       Cohn, M.: Mechanism of cleavage of glucose 1- phosphate. J. Biol. Chem. 180: 771 (1949)

51.       Feldmann, K. and Hull, W.E.: 3,P nuclear magnetic resonance studies of glycogen phosphorylase from rabbit skeletal muscle: Ionization states of pyridoxal 5′-phosphate. Proc. Natl. Acad. Sci. USA 74: 856 (1977)

52.       Withers, S.G., Madsen, N.B., Sykes, B.D., Takagi, M., Shimomura, S. and Fukui, T.: Evidence for the direct phosphate-phosphate interaction between pyridoxal phosphate and substrate in the glycogen phosphorylase catalytic mechanism. J. Biol. Chem. 256: 10759 (1981)

53.       Takagi, M., Fukui T. and Shimomura, S.: Catalytic mechanism of glycogen phosphorylase: Pyridoxal (5′) diphospho(1)-a-D-glucose as a transition-state analogue. Proc. Natl. Acad. Scl. USA 79: 3716 (1982)

54.       Eagles, P.A.M., Iqbal, M., Johnson, L.N., Mosley, J. and Wilson, K.S.: A tetragonal crystal form of phosphorylase b. J. Mot. Biol. 71: 803 (1972)

55.       Johnson, L.N., Madsen, N.B., Mosley, J. and Wilson, K.S.: The crystal structure of phosphorylase b at 6 A resolution. J. Mol. Biol. 90: 703 (1974)

56.       Weber, I.T., Johnson, L.N., Wilson, K.S., Yeates, D.G.R., Wild, D.L and Jenkins, J.A.: Crystallographic studies on the activity of glycogen phosphorylase b. Nature. 274: 433 (1978)

57.       Sansom, M.S.P., Stuart, D.I., Acharya, K.R., Hajdu, J., McLaghlin, P.J. and Johnson, LN.: Glycogen phosphorylase b – the molecular anatomy of a large regulatory enzyme. J. Mol. Struct. 123: 3 (1985)

58.       Oikonomakos, N.G., Johnson, LN.( Acharya, K.R., Stuart, D.I., Barford, D., Hajdu, J., Varvill, K.M., Melpidou, A.E., Papageorgiou, A.C., Graves, D.J. and Palm, D.: Pyridoxal phosphate site in glycogen phosphorylase: Structure in native enzyme and in three derivatives with modified cofactors. Biochemistry 26: 8381 (1987)

59.       Acharya, K.R. et a I.: unpublished results

60.       Titani, Κ., Koide, A., Hermann, J., Ericson, L.H., Kumar. S., Wade. R.D., Walsh, K.A., Neurath, H. and Fischer, E.H.: Complete amino acid sequence of rabbit skeletal muscle glycogen phosphorylase. Proc. Natl. Acad. Sci. USA 74: 4762 (1977)

61.       Nakano, Κ., Hwang, P.K. and Fletterick, R.J.: Complete cDNA sequence for rabbit muscle glycogen phosphorylase. FEBS Lett. 204: 283 (1986)

62.       Sprang, S., Goldsmith, E. and Fletterick, R.: Structure of the nucleotide activation switch in glycogen phosphorylase a. Science 237: 1012 (1987)

63.       Sprang, S.R., Acharya, K.R., Goldsmith, E.J., Stuart, D.I., Varvill, K.M., Fletterick, R.J., Madsen, N.B. and Johnson, L.N.: Structural changes in glycogen phosphorylase induced by phosphorylation. Nature 336: 215 (1988)

64.       Johnson, L.N., Jenkins, J.A., Wilson, K.S., Stura, E.A. and Zanotti, G.: Proposals for the catalytic mechanism of glycogen phosphorylase b prompted by crystallographic studies on glucose-1-phosphate binding. J. Mot. Biol. 140: 565 (1980)

65.       Johnson, L.N., Stura, E.A., Wilson, K.S., Sansom, M.S.P. and Weber, I.T.: Nucleotide binding to glycogen phosphorylase b in the crystal. J. Mot. Biol. 134: 639 (1979)

66.       Stura, E.A., Zanotti, G., Babu, Y.S., Sansom, M.S.P., Stuart, D.I., Wilson, K.S., Johnson, L.N. and Van de Werve, G.: Comparison of AMP and NADH binding to glycogen phosphorylase b. J. Mol. Biol. 170: 529 (1983)

67.       Lorek, A., Wilson, K.S., Sansom, M.S.P., Stuart, D.I., Stura, E.A., Jenkins, J.A., Zanotti. G., Hajdu, J. and Johnson, L.N.: Allosteric ‘interactions of glycogen phosphorylase b. A crystallographic study of glucose-6-phosphate and inorganic phosphate binding to di-imidate cross-linked phosphorylase b. Biochem. J. 218: 45 (1984)

68.       Oikonomakos, N.G., Acharya, K.R., Stuart, D.I., Melpidou, A.E., McLaughlin, P.J. and Johnson, L.N.: Uridine (5’) diphospho(1)-a-D-glucose. A binding study to glycogen phosphorylase b in the crystal. Eur. J. Biochem. 173: 569 (1988)

69.       Oikonomakos, N.G., Acharya, K.R., Melpidou. A.E., Stuart, D.l. and Johnson, L.N.: The binding of β-glycerolphosphate to glycogen phosphorylase b in the crystal. Arch. Biochim. Biophys. 270: 62 (1989)

70.       Johnson, L.N., Acharya, K.R., Stuart, D;l., Barford, D., Oikonomakos, N.G., Hajdu, J. and Varvill, K.M.: Phosphate-recognition sites in catalysis and control of glycogen phosphorylase b. Biochem. Soc. Trans. 15: 1001 (1987)

71.       Johnson, L.N., Cheetham, J., McLaughlin, P.J., Acharya, K.R., Barford, D. and Phillips, D.C.: Protein-oligosaccharide interactions: lysozyme. phosphorylase, amylases. Curr. Top. Microbiol. Immunol. 139: 81 (1988)

72.       Kasvinsky, P.J., Madsen, Ν.Β., Fletterick, R.J. and Sygusch, J.: X-ray crystallographic and kinetic studies on oligosaccharide binding to phosphorylase. J. Biol. Chem. 253: 1290 (1978)

73.       Sotiroudis, T.G., Oikonomakos, N.G. and Evangelopoulos, A.E.: Phoshorylase b covalently bound to glycogen. Eur. J. Biochem: 88: 573 (1978)

74.       Phillip, G„ Gringel, G. and Palm, D.: Rabbit muscle phosphorylase derivatives with oligosaccharides covalently bound to the glycogen storage sites. Biochemistry 21: 3043 (1982)

75.       Melpidou, A.E. and Oikonomakos, N.G.: Effect of glucose-6-P on the catalytic and structural properties of glycogen phosphorylase a. FEBS Lett. 154: 105 (1983)

76.       Black, W.J. and Wang, J.H.: Studies on the allosteric activation of glycogerr phosphorylase b by nucleotides. I. Activation of phosphorylase b by inosine monophosphate. J. Biol. Chem. 243: 5892 (1968)

77.       Barford, D., Schwabe, J.W.R., Oikonomakos, N.G., Acharya, K.R., Hajdu, J., Papageorgiou, A.G., Martin, J.L., Knott, J.C.A., Vasella, A. and Johnson, LN:: Channels at the catalytic site of glycogen phosphorylase b: Binding and kinetic studies with the β- glycosidase inhibitor D-gluconohydroximo-1,5-lactone N-phenylurethane. Biochemistry 27: 6733 (1988)

78.       Barford, D. and Johnson, L.N.: The allosteric transition of glycogen phosphorylase. Nature, in press (1989)

79.       Hwang, P. Stern, M. and Fletterick, R.J.: Purification and crystallization of bovine liver phosphorylase. Biochim. Biophys. Acta 791: 252 (1984)

80.       Oikonomakos, N.G., Melpidou, A.E. and Johnson, LN.: Crystallization of pig skeletal phosphorylase b. Purification, physical and catalytic characterization. Biochim. Biophys. Acta 832: 248 (1985)

81.       Tu, J.I., Jacobson, G.R. and Graves, D.J.: Isotopic effects arid inhibition of polysaccharide phosphorylase by 1,5-gluconolactone. Relationship to the catalytic mechanism. Biochemistry 10: 1229 (1971)

82.       Gold, A.M., Leg rand, E. and Sanchez, G.R.: Inhibition of muscle phosphorylase a by 5-gluconolactone. J. Biol. Chem. 246: 5700 (1971)

83.       Hackert, M.L. and Jacob son, R.A.: The crystal and molecular structure of D-glucono-(1,5)-lactone. Acta Cryst. B27: 203 (1971)

84.       Wang, J.H., Shonka, M.L and Graves, D.J.: The effect of glucose on the sedimentation and catalytic activity of glycogen phosphorylase. Biochem. Biophys. Res. Common. 18: 131 (1965)

85.       Helmreich, E., Michaelides, M.C. and Cori, C.F.: Effect of substrates and substrate analogs on the binding of 5′-adenylic acid to muscle phosphorylase a. Biochemistry 6: 3695 (1967)

86.       Ariki, M. and Fukui, T.: Inhibition of α-giucan phosphbrylase by α-D-glucopyranosyl fluoride. J. Biochem. 78: 1191 (1975)

87.       Ariki, M. and Fukui, T.: Affinity of glucose analoues for α-glucan phosphorylases from rabbit muscle and potato tubers. J. Biochem. 81: 1017 (1977)

88.       Hu, H.Y. and Gold, A.M.: Inhibition of rabbit muscle glycogen phosphorylase by o-D-glucopyranose 1,2-cyclic phosphate. Biochim. Biophys. Acta. 525: 55 (1978)

89.       Kasvinsky, P.J., Shechosky, S. and Fletterick, R.J.: Synergistic regulation of phosphorylase a by glucose and caffeine. J. Biol. Chem. 253: 9102 (1978)

90.       Withers, S.G., Sykes, B.D., Madsen, N.B. and Kasvinsky, P.J.: Identical structural changes induced by glycogen phosphorylase by two nonexclusive allosteric inhibitors. Biochemistry 18: 5342 (1979)

91.       Withers, S.G., Madsen, N.B. and Sykes, B.D.: Active form of pyridoxal phosphate in glycogen phosphorylase. Phosphorus-31 nuclear magnetic resonance investigation. Biochemistry 20: 1748 (1981)

92.       Kasvinsky, P.J.: The effect of AMP on inhibition of muscle phosphorylase a by glucose derivatives. J. Biol. Chem. 25: 10805 (1982)

93.       Madsen, N.B., Shechosky, S. and Fletterick, R.J.: Site- site interactions in glycogen phosphorylase b probed by ligands specific for each site. Biochemistry 22: 4460 (1983)

94.       Jenkins, J.A., Johnson, LN., Stuart, D.I., Stura, E.A., Wilson, K.S. and Zanotti, G.: Phosphorylase: control and activity. Phil. Trans. Roy. Soc. B293: 23 (1981)

95.       McLaughlin, P.J., Stuart, D.I., Klein, H.W., Oikonomakos, N.G. and Johnson, LN.: Substrate-cofactor interactions for glycogen phosphorylase b: A binding study in the crystal with heptenitol and heptuIose-2-phosphate. Biochemistry 23: 5862 (1984)

96.       Klein, H.W., Palm, D. and Helmreich, E.J.M.: General acid-base catalysis of α-glucan phosphorylases: stereospecific glucosyl transfer from D-glucal is a pyridoxal 5′-phosphate and orthophosphate (arsenate) dependent reaction. Biochemistry 21: 6675 (1982)

97.       Palm, D., Blumenauer, G„ Klein, H.W. and Blanc- Muesser, M.: α-glucan phosphorylases catalyse the glucosyl transfer from α-D-glycosyl fluoride to oligosaccharides. Biochem. Biophys. Res. Commun. 111: 530 (1983)

98.       Klein, H.W., Im, M.J., Palm, D. and Helmreich, E.J.M.: Does pyridoxal 5′-phosphate function in glycogen phosphorylase as an electrophilic or a general acid catalyst? Biochemistry 23: 5853 (1984)

99.       Hehre, E.J., Brewer, C.F., Uchiyama, T., Schlesselmann, P. and Lehmann, J.: Scope and mechanism of carbohydrase action. Stereospecific hydration of 2,6-an- hydro-1-deoxy-D-gluco-hept-1-enitol catalysed by a- and β-glucosidases and an inverting exo-a-glucanase. Biochemistry 19: 3557 (1980)

100.     Beer, D. and Vasella, A.: Aldonhydroximo-lactones. Preparation and determination of configuration. Helv. Chim. Acta 68: 2254 (1985)

101.     Beer, D. and Vasella, A.: Inhibition of emulsin by D- gluconhydroximo-1,5-lactone and refated compounds. Helv. Chim. Acta 69: 267 (1986)

102.     Papageorgiou, A.C., Oikonomakos, N.G. and Leonidas, D.D.: Inhibition of rabbit muscle glycogen phosphorylase by D-gluconohydroximo-1,5-lactone-N-phenylurethane. Arch. Biochem. Biophys., 272: 376 (1989)

103.     Papageorgiou, A.C. et al., unpublished results.

104.     Hedrick, J.L, Shaltiel, S. and Fischer, E.H.: On the role of pyridoxal 5′-phosphate in phosphorylase III. Physicochemical properties and reconstitution of apophosphorylase b. Biochemistry 5: 2117 (1966)

105.     Fischer, E.H., Kent, A.B., Synder, E.R. and Krebs, E.G.: The reaction of sodium borohydride with muscle phosphorylase. J. Am. Chem. Soc. 80: 2906 (1958)

106.     Fischer, E.H.: Binding of vitamin Becoenzymes and labelling of active site of enzymes by sodium borohydride reduction. In: Structure and Activity of Enzymes, (T.W. Goodwin, J.I. Harris and B.S. Hartley, eds), p. 111, B.S. Sympos. No. 1, Fedn European Biochemical Societies, London, Academic Press, 1964

107.     Kastensehmidt, L.L., Kastenschmidt, J. and Helmreich, E.: Subunit interactions and their relationship to the allosteric properties of rabbit skeletal muscle phosphorylase b. Biochemistry 7: 3590 (1968)

108.     Shaltiel, S., Hedrick, J.L., Pocker, A. and Fischer, E.H.: Reconstitution of apophosphorylase with pyridoxal 5′-phosphate analogs. Biochemistry 8: 5189 (1969)

109.     Pfeuffer, T., Ehrlich, J. and Helmreich, E.: Role of pyridoxal 5′-phosphate in glycogen phosphorylase: I. Synthesis of 3′-0-methylpyridoxal 5′-phosphate N-oxtde and pyridoxal 5′-phosphate monomethyl ester and the conversion of the N-oxide to pyridoxal 5′-phosphate by apophosphorylase b from rabbit skeletal muscle. Biochemistry 11: 2125 (1972)

110.     Pfeuffer, T., Ehrlich, J. and Helmreich, E.: Role of pyridoxal 5′-phosphate in glycogen phosphorylase-II. Mode of binding of pyridoxal 5′-phosphate to apophosphorylase b and the aggregation state of reconstituted phosphorylase proteins. Biochemistry 11: 2136 (1972)

111.     Vidgoff, J.M., Pocker, A., Hullar, T.L and Fischer, E.H.: Interaction of muscle glycogen phosphorylase with pyridoxal 5′-phosphonate. Biochem. Biophys. Res. Commun. 57: 1166 (1974)

112.     Parrish, R.F., Uhing, R.J. and Graves, D.J.: Effect of phosphate analogues on the activity of pyridoxal reconstituted glycogen phosphorylase. Biochemistry 16: 4824 (1977)

113.     Shimomura, S. and Fukui, T.: Characterization of the pyridoxal phosphate site in glycogen phosphorylase b from rabbit muscle. Biochemistry 17: 5359 (1978)

114.     Yan, S.C.B., Uhing, R.J., Parrish, R.F., Metzler, D.E. and Graves, D.J.: A role for pyridoxal phosphate in the control of dephosphorylation of phosphorylase a. J. Biol. Chem. 254: 8263 (1979)

115.     Chang, Y.C. and Graves, D.J.: Use of 6-fluoroderivatives of pyridoxal and pyridoxal phosphate in the study of the coenzyme function in glycogen phosphorylase. J. Biol. Chem. 260: 2709 (1985)

116.     Chang, Y.C., Scott, R.D. and Graves, D.J.: Function of pyridoxal 5′-phosphate in glycogen phosphorylase: A model study using 6-fluoro-5′-pyridoxal- and 5′-deoxy-pyridoxal-reconstituted enzymes. Biochemistry 26: 360 (1987)

117.     Johnson, L.N., Oikonomakos, N.G., Acharya, K.R., Stuart, D.I., Barford, D., Hajdu, J. and Varvill, K.M.: The role of the pyridoxal phosphate in glycogen phosphorylase b. In: Biochemistry of Vitamin B6 (B): proceedings of the 7th Internat. Congress on Chem. and Biolog. Aspects of Vitamin Be Catalysis (T.P. Korpella and P. Christen, eds), p. 255, Birkhauser Verlag, Basel-Boston, 1987

118.     Chang, Y.C., McCalmont, T. and Graves, O.J.: Function of the 5′-phosphoryl group of pyridoxal 5′- phosphate in phosphorylase: A study using pyridoxal- reconstituted enzyme as a model system. Biochemistry 22: 4987 (1983)

119.     M. Tokushige (ed.): Selected Papers in Biochemistry, Vol. 8, Allosteric Regulation, University Park Press, Baltimore, London, Tokyo, 1971

120.     Monod, J., Wyman, J. and Changeux, J.-P.: On the nature of allosteric transitions: a plausible model. J. Mot. Biol. 12: 88 (1965)

121.     Koshland, D.E., Nemethy, G. and Filmer, O.: Comparison of experimental data and theoretical models in proteins containing subunits. Biochemistry 5: 365 (1966)

122.     Busby, S.J.W. and Radda, G.K.: Regulation of the glycogen phosphorylase system. Curr. Top. Cell. Regul. 10: 89 (1976)

123.     Madsen, N.B., Kasvinsky, P.J. and Fletterick, R.J.: Allosteric transitions of phosphorylase a and the regulation of glycogen metabolism. J. Biol. Chem. 253: 9097 (1978)

124.     Battersby, M.K. and Radda, G.K.: Intersubunit trans-mission of ligand effects in the glycogen phosphorylase b dimer. Biochemistry 18: 3774 (1979)

125.     Madsen, N.B. and Shechosky, S.: Allosteric properties of phosphorylase b. II. Comparison with a kinetic model. J. Biol Chem. 242: 3301 (1967)

126.     Madsen, N.B., Avramovic-Zikic, O., Lue, P.F. and Honikel, H.O.: Studies on allosteric phenomena in glycogen phosphorylase b. Mot. Cell. Biochem. 11: 35 (1976)

127.     Kasvinsky, P.J., Madsen, N.B., Sygusch, J. and Fletterick, R.J.: The regulation of glycogen phosphorylase a by nucleotide derivatives. J. Biol Chem. 253: 3343 (1978)

128.     Steiner, R.F., Greer, L., Bath, R. and Oton, J.: Structural changes in glycogen phosphorylase b induced by the binding of glucose and caffeine. Biochim. Biophys. Acta 611: 269 (1980)

129.     Wang, H.H., Shonka, M.L. and Graves, D.J.: Influence of carbohydrates on phosphorylase structure and activity. I. Activation by preincubation with glycogen. Biochemistry 11: 2296 (1965)

130.     Metzger, B., Helmreich, E. and Glaser, L.: The mechanism of activation of skeletal muscle phosphorylase a by glycogen. Proc. Natl. Acad. Sci. USA 57: 994 (1967)

131.     Sprang, S.R., Goldsmith, E.J., Fletterick, R.J., Withers, S.G. and Madsen, N.B.: Catalytic site of glycogen phosphorylase: structure of the T state and specificity for α-D-glucose. Biochemistry, 21: 5364 (1982)

132.     Withers, S.G., Madsen, N.B., Sprang, S.R. and Fletterick, R.J.: Catalytic site of glycogen phosphorylase: structural changes during activation and mechanistic implications. Biochemistry 21: 5372 (1982)

133.     Madsen, N.B.: The inhibition of glycogen phosphorylase by uridine diphosphate glucose. Biochem. Bio- phys. Res. Commun. 6: 310 (1961)

Relative Papers

Online ISSN 1011-6575

Άρθρα Δημοσιευμένα σε αυτό το Περιοδικό Καταχωρούνται στα:

Articles published in this Journal are Indexed or Abstracted in: • Chemical Abstracts • Elsevier’s Bibliographic Databases: Scopus, EMBASE, EMBiology, Elsevier BIOBASE SCImago Journal and Country Rank Factor

Τι είναι η Επιθεώρηση Κλινικής Φαρμακολογίας και Φαρμακοκινητικής-Διεθνής Έκδοση-Οδηγίες προς τους Συγγραφείς –
What is Epitheorese Klinikes Farmakologias
και Farmakokinetikes-International Edition-Instrunctions to Authors

Άρθρα Δημοσιευμένα στην Επιθεώρηση Κλινικής Φαρμακολογίας και Φαρμακοκινητικής-Διεθνής Έκδοση –
Articles Published in Epitheorese Klinikes Farmakologias
και Farmakokinetikes-International Edition

Συντακτικη Επιτροπή-Editorial Board

ΕΤΗΣΙΑ ΣΥΝΔΡΟΜΗ 1989 – ANNUAL SUBSCRIPTION 1989
Γλώσσα Πλήρους Κειμένου – Full Text Language Αγγλικά, Γαλλικά – English, French
Παραγγελία – Αγορά – Order – Buy Ηλεκτρονική Μορφή: pdf (70 €) – Digital Type: pdf (70 €)

pharmakonpress[at]pharmakonpress[.]gr

Έντυπη Μορφή (70 € + έξοδα αποστολής) – Printed Type (70 € + shipping)

pharmakonpress[at]pharmakonpress[.]gr

 

 

Bookmark the permalink.

Comments are closed.