Contribution of amino acid region 334-335 from factor Va heavy chain to the catalytic efficiency of prothrombinase

Biochemistry

Volumn 47, Issue 26, 2008, Pages 6840-6850

  Barhoover, Melissa A ^a,d   Orban, Tivadar ^a   Beck, Daniel O ^a,c   Bukys, Michael A ^a   Kalafatis, Michael ^a,b  

^a CLEVELAND STATE UNIVERSITY   (United States)

^b LERNER RESEARCH INSTITUTE   (United States)

^c UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^d HAMNER INSTITUTES FOR HEALTH SCIENCES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINATION; AMINES; AMINO ACIDS; HEALTH;

ACID REGION; CATALYTIC EFFICIENCIES; HEAVY CHAIN (VH); PROTHROMBINASE;

ORGANIC ACIDS;

AMINO ACID; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 5A;

ARTICLE; CATALYSIS; ENZYME BINDING; ENZYME STRUCTURE; KINETICS; PRIORITY JOURNAL; PROTEIN INTERACTION;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; CATALYSIS; CERCOPITHECUS AETHIOPS; COS CELLS; ENZYME ACTIVATION; FACTOR VA; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; THROMBIN; THROMBOPLASTIN;

EID: 46049110107     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800057r     Document Type: Article

References (55)

1. Kalafatis, M., Egan, J. O., van't Veer, C., Cawthern, K. M., and Mann, K. G. (1997) The regulation of clotting factors. Crit. Rev. Eukaryotic Gene Expression 7, 241-280.
2. Kalafatis, M., and Mann, K. G. (2001) Factor V: Dr. Jeckyll and Mr. Hyde. Adv. Exp. Med. Biol. 489, 31-43.
3. Rosing, J., Zwaal, R. F., and Tans, G. (1986) Formation of meizothrombin as intermediate in factor Xa-catalyzed prothrombin activation. J. Biol. Chem. 261, 4224-4228.
4. Owen, W. G., Esmon, C. T., and Jackson, C. M. (1974) The conversion of prothrombin to thrombin. I. Characterization of the reaction products formed during the activation of bovine prothrombin. J. Biol. Chem. 249, 594-605.
5. Esmon, C. T., Owen, W. G., and Jackson, C. M. (1974) The conversion of prothrombin to thrombin. II. Differentiation between thrombin- and factor Xa-catalyzed proteolyses. J. Biol. Chem. 249, 606-611.
6. Esmon, C. T., and Jackson, C. M. (1974) The conversion of prothrombin to thrombin. III. The factor Xa-catalyzed activation of prothrombin. J. Biol. Chem. 249, 7782-7790.
7. Krishnaswamy, S., Church, W. R., Nesheim, M. E., and Mann, K. G. (1987) Activation of human prothrombin by human prothrombinase. Influence of factor Va on the reaction mechanism. J. Biol. Chem. 262, 3291-3299.
8. Nesheim, M. E., Taswell, J. B., and Mann, K. G. (1979) The contribution of bovine Factor V and Factor Va to the activity of prothrombinase. J. Biol. Chem. 254, 10952-10962.
9. Nesheim, M. E., and Mann, K. G. (1983) The kinetics and cofactor dependence of the two cleavages involved in prothrombin activation. J. Biol. Chem. 258, 5386-5391.
10. Esmon, C. T., Owen, W. G., and Jackson, C. M. (1974) A plausible mechanism for prothrombin activation by factor Xa, factor Va, phospholipid, and calcium ions. J. Biol. Chem. 249, 8045-8047.
11. Downing, M. R., Butkowski, R. J., Clark, M. M., and Mann, K. G. (1975) Human prothrombin activation. J. Biol. Chem. 250, 8897-8906.
12. Butkowski, R. J., Elion, J., Downing, M. R., and Mann, K. G. (1977) Primary structure of human prethrombin 2 and α-thrombin. J. Biol. Chem. 252, 4942-4957.
13. 2+ binding and activation kinetics. J. Biol. Chem. 250, 2150-2156.
14. Myrmel, K. H., Lundblad, R. L., and Mann, K. G. (1976) Characteristics of the association between prothrombin fragment 2 and α-thrombin. Biochemistry 15, 1767-1773.
15. Brufatto, N., and Nesheim, M. E. (2003) Analysis of the kinetics of prothrombin activation and evidence that two equilibrating forms of prothrombinase are involved in the process. J. Biol. Chem. 278, 6755-6764.
16. Suzuki, K., Dahlback, B., and Stenflo, J. (1982) Thrombin-catalyzed activation of human coagulation factor V. J. Biol. Chem. 257, 6556-6564.
17. Nesheim, M. E., Foster, W. B., Hewick, R., and Mann, K. G. (1984) Characterization of Factor V activation intermediates. J. Biol. Chem. 259, 3187-3196.
18. Adams, T. E., Hockin, M. F., Mann, K. G., and Everse, S. J. (2004) The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function. Proc. Natl. Acad. Sci. U.S.A. 101, 8918-8923.
19. Orban, T., Kalafatis, M., and Gogonea, V. (2005) Completed three-dimensional model of human coagulation factor Va. Molecular dynamics simulations and structural analyses. Biochemistry 44, 13082-13090.
20. Kalafatis, M., Xue, J., Lawler, C. M., and Mann, K. G. (1994) Contribution of the heavy and light chains of factor Va to the interaction with factor Xa. Biochemistry 33, 6538-6545.
21. Luckow, E. A., Lyons, D. A., Ridgeway, T. M., Esmon, C. T., and Laue, T. M. (1989) Interaction of clotting factor V heavy chain with prothrombin and prethrombin 1 and role of activated protein C in regulating this interaction: Analysis by analytical ultracentrifugation. Biochemistry 28, 2348-2354.
22. Kalafatis, M., and Mann, K. G. (2001) The Role of the Membrane in the Inactivation of Factor Va by Plasmin: Amino Acid Region 307-348 of Factor V Plays a Critical Role in Factor Va Cofactor Function. J. Biol. Chem. 276, 18614-18623.
23. Kalafatis, M., and Beck, D. O. (2002) Identification of a binding site for blood coagulation factor Xa on the heavy chain of factor Va. Amino acid residues 323-331 of factor V represent an interactive site for activated factor X. Biochemistry 41, 12715-12728.
24. Heeb, M. J., Kojima, Y., Hackeng, T. M., and Griffin, J. H. (1996) Binding sites for blood coagulation factor Xa and protein S involving residues 493-506 in factor Va. Protein Sci. 5, 1883-1889.
25. Jenny, R. J., Pittman, D. D., Toole, J. J., Kriz, R. W., Aldape, R. A., Hewick, R. M., Kaufman, R. J., and Mann, K. G. (1987) Complete cDNA and derived amino acid sequence of human factor V. Proc. Natl. Acad. Sci. U.S.A. 84, 4846-4850.
26. Guinto, E. R., Esmon, C. T., Mann, K. G., and MacGillivray, R. T. (1992) The complete cDNA sequence of bovine coagulation factor V. J. Biol. Chem. 267, 2971-2978.
27. Yang, T. L., Cui, J., Rehumtulla, A., Yang, A., Moussalli, M., Kaufman, R. J., and Ginsburg, D. (1998) The structure and function of murine factor V and its inactivation by protein C. Blood 91, 4593-4599.
28. Grimm, D. R., Colter, M. B., Braunschweig, M., Alexander, L. J., Neame, P. J., and Kim, H. K. (2001) Porcine factor V: cDNA cloning, gene mapping, three-dimensional protein modeling of membrane binding sites and comparative anatomy of domains. Cell. Mol. Life Sci. 58, 148-159.
29. Singh, L. S., Bukys, M. A., Beck, D. O., and Kalafatis, M. (2003) Amino acids Glu323, Tyr324, Glu330, and Val331 of factor Va heavy chain are essential for expression of cofactor activity. J. Biol. Chem. 278, 28335-28345.
30. Bukys, M., Kim, P. Y., Nesheim, M. E., and Kalafatis, M. (2006) A Control Switch for Prothrombinase. Characterization of a Hirudin-Like Pentapeptide From the COOH Terminus of Factor Va Heavy Chain that Regulates the Rate and Pathway for Prothrombin Activation. J. Biol. Chem. 281, 39194-39204.
31. Bukys, M. A., Blum, M. A., Kim, P. Y., Brufatto, N., Nesheim, M. E., and Kalafatis, M. (2005) Incorporation of factor Va into prothrombinase is required for coordinated cleavage of prothrombin by factor Xa. J. Biol. Chem. 280, 27393-27401.
32. Erdogan, E., Bukys, M. A., Orfeo, T., Mann, K. G., and Kalafatis, M. (2007) Identification of an inactivating cleavage site for α-thrombin on the heavy chain of factor Va. Thromb. Haemostasis 98, 998-1006.
33. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
34. Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from Polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76, 4350-4354.
35. Erdogan, E., Bukys, M. A., and Kalafatis, M. (2008) The contribution of amino acid residues 1508-1515 of factor V to light chain generation. J. Thromb. Haemostasis 6, 118-124.
36. Krishnaswamy, S. (1992) The interaction of human factor VIIa with tissue factor. J. Biol. Chem. 267, 23696-23706.
37. Krishnaswamy, S., Williams, E. B., and Mann, K. G. (1986) The binding of activated protein C to factors V and Va. J. Biol. Chem. 261, 9684-9693.
38. Ackers, G. K., and Smith, F. R. (1985) Effects of site-specific amino acid modification on protein interactions and biological function. Annu. Rev. Biochem. 54, 597-629.
39. LiCata, V. J., and Ackers, G. K. (1995) Long-range, small magnitude nonadditivity of mutational effects in proteins. Biochemistry 34, 3133-3139.
40. Wells, J. A. (1990) Additivity of mutational effects in proteins. Biochemistry 29, 8509-8517.
41. Mildvan, A. S., Weber, D. J., and Kuliopulos, A. (1992) Quantitative interpretations of double mutations of enzymes. Arch. Biochem. Biophys. 294, 327-340.
42. Mildvan, A. S. (2004) Inverse thinking about double mutants of enzymes. Biochemistry 43, 14517-14520.
43. Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18, 2714-2723.
44. Berendsen, H. J. C., van der Spoel, D., and van Drunen, R. (1995) GROMACS: A message-passing parallel molecular dynamics implementation. Comput. Phys. Commun. 91, 43-56.
45. Lindahl, E., Hess, B., and van der Spoel, D. (2001) GROMACS 3.0: A package for molecular simulation and trajectory analysis. J. Mol. Model. 7, 306-317.
46. Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., and Hermans, J. (1981) Interaction models for water in relation to protein hydration, in Intermolecular Forces (Pullman, B., and Reidel, D., Eds.) pp 331-342, Kluwer Academic Publishers, Dordrecht, The Netherlands.
47. van Gunsteren, W. F., and Berendsen, H. J. C. (1987) Gromos-87 Manual, Biomos BV, Groningen, The Netherlands.
48. Hess, B., Bekker, H., Berendsen, H. J. C., and Fraaije, J. G. E. M. (1997) LINCS: A linear constraint solver for molecular simulations. J. Comput. Chem. 18, 1463-1472.
49. Darden, T., York, D., and Pedersen, L. (1993) Particle mesh Ewald: An N • log(N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089-10092.
50. Essmann, U., Perera, L., Berkowitz, M. L., Darden, T., Lee, H., and Pedersen, L. G. (1995) A smooth particle mesh Ewald method. J. Chem. Phys. 103, 8577-8593.
51. Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., DiNola, A., and Haak, J. R. (1984) Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81, 3684-3690.
52. Parrinello, M., and Rahman, A. (1980) Structure and pair potentials: A molecular-dynamics study. Phys. Rev. Lett. 45, 1196-1199.
53. Segal, I. H. (1993) Enzyme Kinetics, pp 170-178, John Wiley & Sons, Inc., New York.
54. Kalafatis, M., Beck, D. O., and Mann, K. G. (2003) Structural requirements for expression of factor Va activity. J. Biol. Chem. 278, 33550-33561.
55. Beck, D. O., Bukys, M. A., Singh, L. S., Szabo, K. A., and Kalafatis, M. (2004) The contribution of amino acid region ASP695-TYR698 of factor V to procofactor activation and factor Va function. J. Biol. Chem. 279, 3084-3095.