Kinetic analysis and modelling of the allosteric behaviour of liver and muscle glycogen phosphorylases

Journal of Molecular Recognition

Volumn 19, Issue 5, 2006, Pages 451-457

  Cuadri Tomé, Celia ^a   Barón, Carmen ^a   Jara Pérez, Vicente ^a   Parody Morreale, Antonio ^b   Martinez, Jose C ^b,c   Cámara Artigas, Ana ^a  

^a UNIVERSITY OF ALMERÍA   (Spain)

^b UNIVERSITY OF GRANADA   (Spain)

^c UNIVERSITY OF GRANADA   (Spain)

Author keywords

Allosterism; Cooperativity; Glycogen phosphorylase; Xanthine

Indexed keywords

1 METHYLXANTHINE; 1-METHYLXANTHINE; CAFFEINE; GLYCOGEN PHOSPHORYLASE; XANTHINE DERIVATIVE;

ALLOSTERISM; ANIMAL; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; METABOLISM; PROTEIN BINDING; RABBIT;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; ANIMALS; CAFFEINE; GLYCOGEN PHOSPHORYLASE, LIVER FORM; GLYCOGEN PHOSPHORYLASE, MUSCLE FORM; KINETICS; MODELS, MOLECULAR; PROTEIN BINDING; RABBITS; XANTHINES;

EID: 33748939129     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.772     Document Type: Article

References (32)

1. Artigas AC, Baron C, Parody-Morreale A. 1994. Purification of two forms of bovine liver glycogen phosphorylase b with distinct subunit composition. Protein Expr. Purif. 5: 157-163.
2. Artigas AC, Baron C, Parody-Morreale A. 1995. Molecular studies of glycogen phosphorylase b from bovine liver. Int. J. Biol. Macromol. 17: 67-73.
3. Barford D, Hu SH, Johnson LN. 1991. Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP. J. Mol. Biol. 218: 233-260.
4. Bevington PR, Robinson DK. 1991. Data Reduction and Error Analysis for the Physical Sciences. McGraw-Hill Companies: New York.
5. Brunger AT, Adams PD, Clore GM, Delano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. 1998. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54: 905-921.
6. Buc MH, Ullmann A, Goldberg M, Buc H. 1971. Molecular weight and extinction coefficient of glycogen phosphorylase-B from rabbit muscle. Biochimie 53: 283-289.
7. Buchbinder JL, Rath VL, Fletterick RJ. 2001. Structural relationships among regulated and unregulated phosphorylases. Annu. Rev. Biophys. Biomol. Struct. 30: 191-209.
8. Camara-Artigas A, Parody-Morreale A, Baron C. 1997. Analogous activation of bovine liver glycogen phosphorylase by AMP and IMP. Int. J. Biochem. Cell Biol. 29: 849-856.
9. Cohen P. 1973. Subunit structure of rabbit-skeletal-muscle phosphorylase kinase, and molecular basis of its activation reactions. Eur. J. Biochem. 34: 1-14.
10. DeLano WL. 2005. The PyMOL molecular graphics system. DeLano Scientific LLC, San Carlos, CA, USA on World Wide Web. Ref Type: Computer Program
11. Fischer EH, Krebs EG. 1958. The isolation and crystallization of rabbit skeletal muscle phosphorylase b. J. Biol. Chem. 231: 65-72.
12. Fiske CH, Subbarow Y. 1925. The colorimetric determination of phosphorus. J. Biol. Chem. 66: 375-400.
13. Garcia-Fuentes L, Camara-Artigas A, Lopez-Mayorga O, Baron C. 1996. Thermodynamic characterization of 5′-AMP binding to bovine liver glycogen phosphorylase a. J. Biol. Chem. 271: 27569-27574.
14. Hedrick JL, Fischer EH. 1965. On the role of pyridoxal 5′-phosphate in phosphorylase. I. Absence of classical vitamin B6 - dependent enzymatic activities in muscle glycogen phosphorylase. Biochemistry 4: 1337-1343.
15. Hubbard SJ, Thornton JM. NACCESS. 1993. Department of Biochemistry and Molecular Biology, University College London. Ref Type: Computer Program.
16. Johnson LN. 1992. Glycogen phosphorylase: control by phosphorylation and allosteric effectors. FASEB J. 6: 2274-2282.
17. Johnson LN, O'Reilly M. 1996. Control by phosphorylation. Curr. Opin. Struct. Biol. 6: 762-769.
18. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47: 110-119.
19. Kabsch W. 1976. Solution for best rotation to relate 2 sets of vectors. Acta Crystallogr. A 32: 922-923.
20. Kasvinsky PJ, Shechosky S, Fletterick RJ. 1978. Synergistic regulation of phosphorylase a by glucose and caffeine. J. Biol. Chem. 253: 9102-9106.
21. Kilhman B, Overgaard-Hansen K. 1955. Inhibition of muscle phosphorylase by methylated oxypurines. Exp. Cell Res. 8: 252-255.
22. Koshland DE, Nemethy G, Filmer D. 1966. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5: 365-385.
23. Krebs EG. 1981. Phosphorylation and dephosphorylation of glycogen phosphorylase: a prototype for reversible covalent enzyme modification. Curr. Top. Cell Regul. 18: 401-419.
24. Lee B, Richards FM. 1971. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55: 379-400.
25. Madson NB, Shechosky S, Fletterick RJ. 1983. Site-site interactions in glycogen phosphorylase b probed by ligands specific for each site. Biochemistry, 22: 4460-4465.
26. Makhatadze GI, Privalov PL. 1995. Energetics of protein structure. Adv. Protein Chem. 47: 307-425.
27. Monod J, Wyman J, Changeux JP. 1965. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12: 88-118.
28. Newgard CB, Hwang PK, Fletterick RJ. 1989. The family of glycogen phosphorylases: structure and function. Crit Rev. Biochem. Mol. Biol. 24: 69-99.
29. Palencia A, Cobos ES, Mateo PL, Martinez JC, Luque I. 2004. Thermodynamic dissection of the binding energetics of proline-rich peptides to the Abl-SH3 domain: implications for rational ligand design. J. Mol. Biol. 336: 527-537.
30. Soman G, Philip G. 1975. The nature of the binding site for aromatic compounds in glycogen phosphorylase b. Biochem. J. 147: 369-371.
31. Sprang SR, Goldsmith EJ, Fletterick RJ, Withers SG, Madsen NB. 1982. Catalytic site of glycogen phosphorylase: structure of the T state and specificity for alpha-D-glucose. Biochemistry 21: 5364-5371.
32. Tsitsanou KE, Skamnaki VT, Oikonomakos NG. 2000. Structural basis of the synergistic inhibition of glycogen phosphorylase a by caffeine and a potential antidiabetic drug. Arch. Biochem. Biophys. 384: 245-254.