Advertisement

Linear Free Energy Relationships in Enzymology

  • Jack F. Kirsch

Abstract

The primary objective of the application of the various linear free energy relationships in enzymology, as is often the case in non-enzymic studies of this type, is the elucidation of reaction mechanism. Thus, it is expected that systematic perturbations in the structure of the substrate for a particular enzyme will affect the catalysed reaction in such a manner as to provide evidence concerning the mode of catalysis, which can be rationally interpreted.

Keywords

Rate Coefficient Nicotinamide Adenine Dinucleotide Hippuric Acid Acyl Moiety Phenyl Acetate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    R. L. Blakeley, J. A. Hinds, H. E. Kunze, E. C. Webb, and B. Zerner, Biochemistry, 8, 1991 (1969)CrossRefGoogle Scholar
  2. 2.
    W. N. Fishbein, T. S. Winter, and J. D. Davidson, J. Biol. Chem., 240, 2402 (1965)Google Scholar
  3. 3.
    E. Fischer, Chem. Ber., 27, 2985 (1894)CrossRefGoogle Scholar
  4. 4.
    D. E. Koshland and K. E. Neet, Ann. Rev. Biochem., 37, 359 (1968)CrossRefGoogle Scholar
  5. 5.
    R. L. VanEtten, J. F. Sebastian, G. A. Clowes, and M. L. Bender, J. Amer. Chem. Soc., 89, 3242 (1967)CrossRefGoogle Scholar
  6. 6.
    K. Landsteiner, The Speciiicity of Serological Reactions, p. 169 ( Dover Publications, New York, 1962 )Google Scholar
  7. 7.
    L. Michaelis and M. L. Menten, Biochem. Z., 49, 333 (1913)Google Scholar
  8. 8.
    M. Eigen and G. G. Hammes, Adv. Enzymol., 25, 1 (1963); G. G. Hammes, Adv. Protein Chem., 23, 1 (1968)Google Scholar
  9. 9.
    W. P. Jencks, Catalysis in Chemistry and Enzymology, pp. 323–459 ( McGraw-Hill, New York, 1969 )Google Scholar
  10. 10.
    D. M. Blow and T. A. Steitz, Ann. Rev. Biochem., 39, 63 (1970)CrossRefGoogle Scholar
  11. 11.
    W. Kauzmann, Adv..Protein Chem., 14, 1 1959 )CrossRefGoogle Scholar
  12. 12.
    G. Nemethy and H. A. Scheraga, J. Phys.(Chem., 66, 1773 (1962); 67, 2888 (1963); G. Nemethy, Angew. Chem. Internat. Edn., 6, 195 (1967); GE, 260Google Scholar
  13. 13.
    A. Wishnia, Proc. Nat. Acad. Sci. U.S.A., 48, 2200 (1962)CrossRefGoogle Scholar
  14. 14.
    M. R. V. Sahyun, Nature, 209, 613 (1966)CrossRefGoogle Scholar
  15. 15.
    C. Hansch, Accts. Chem. Res., 2, 232 (1969)CrossRefGoogle Scholar
  16. 16.
    C. Hansch, K. Kiehs, and G. L. Lawrence, J. Amer. Chem. Soc., 87, 5770 (1965)CrossRefGoogle Scholar
  17. 17.
    F. Helmer, K Kiehs, and C. Hansch, Biochemistry, 7, 2858 (1968)CrossRefGoogle Scholar
  18. 18.
    K. Kiehs, C. Hansch, and L. Moore, Biochemistry, 5, 2602 (1966)CrossRefGoogle Scholar
  19. 19.
    I. B. Wilson in The Enzymes, Vol. 4, p. 501, P. D. Boyer, H. Lardy, and K. Myrbäck,. (Academic Press, New York, 2nd edn., 1960 )Google Scholar
  20. 20.
    R. M. Krupka, Biochemistry, 5, 1988 (1966)Google Scholar
  21. 21.
    I. B. Wilson, Biol. Chem., 197, 215 (1952)Google Scholar
  22. 22.
    F. Bergmann and R. Segal, Biochem. J., 58, 692 (1954)Google Scholar
  23. 23.
    V. H. Bockendahl, T. M. Müller, and H. Verfürth, Hoppe-Seyler’s Z. Physiol. Chem., 348, 1027 (1967)CrossRefGoogle Scholar
  24. 24.
    B. Belleau and J. L. Lavoie, Can. J. Biochem., 46, 1397 (1968)CrossRefGoogle Scholar
  25. 25.
    B. Belleau and V. DiTullio, J. Amer. Chem. Soc., 92, 6320 (1970)CrossRefGoogle Scholar
  26. 26.
    J. R. Knowles, J. Theoret. Biol, 9, 213 (1965)CrossRefGoogle Scholar
  27. 27.
    A. J. Hymes, D. A. Robinson, and W. J. Canady, J. Biol. Chem., 240, 134 (1965)Google Scholar
  28. 28.
    R. Wildnauer and W. J. Canady, Biochemistry, 5, 2885 (1966)CrossRefGoogle Scholar
  29. 29.
    I. V. Berezin, A. V. Levashov, and K. Martinek, FEBS Letters, 7, 20 (1970)CrossRefGoogle Scholar
  30. 30.
    B. M. Anderson, M. L. Reynolds, and C. D. Anderson, Biochim. Biophys. Acta, 99, 46 (1965)Google Scholar
  31. 31.
    C. S. Tsai, Can. J. Biochem., 46, 381 (1968)CrossRefGoogle Scholar
  32. 32.
    B. M. Anderson and E. C. Vasini, Biochemistry, 9,3348 (1970), and references therein.Google Scholar
  33. 33.
    J. L. Bada, B. P. Luyendyk, and J. B. Maynard, Z. Physiol. Chem, 170, 730 (1970)Google Scholar
  34. 34.
    M. Dixon and E. C. Webb, Enzymes, p. 772 (Academic Press, New York, 2nd edn., 1964), and references therein.Google Scholar
  35. 35.
    D. R. Storm and D. E. Koshland, Proc. Nat. Acad. Sci. U.S.A., 66, 445 (1970)CrossRefGoogle Scholar
  36. 36.
    Reference 9, Chapter 5 and references therein.Google Scholar
  37. 37.
    R. Lumry and R. Biltonin in Biological Macromolecules, Vol. 2, p. 65, S. N. TimashefF and G. D. Fasman, ( Marcel Dekker, New York, 1969 ).Google Scholar
  38. 38.
    B. H. J. Hofstee, J. Biol. Chem., 207, 219 (1954)Google Scholar
  39. 39.
    R. Lumry in The Enzymes, Vol. 1, p. 157, P. D. Boyer, H. Lardy, and K. Myrbäck, (Academic Press, New York, 2nd edn., 1959 )Google Scholar
  40. 40.
    B. H. J. Hofstee, Biochim. Biophys. Acta, 32, 182 (1959)CrossRefGoogle Scholar
  41. 41.
    C. Niemann, Z. Physiol. Chem, 143, 1287 (1964)Google Scholar
  42. 42.
    M. L. Bender and F. J. Kezdy, Ann. Rev. Biochem., 34, 49 (1965)CrossRefGoogle Scholar
  43. 43.
    For recent reviews see (a) G. P. Hess, J. McConn, E. Ku, and G. McConkey, Phil. Trans. Roy. Soc. (B), 257, 89 (1970); (b) S. A. Bernhard and H. Gutfreund, Phil. Trans. Roy. Soc. (B), 257, 105 (1970)Google Scholar
  44. 44.
    G. Lowe, Phil. Trans. Roy. Soc. (B), 257, 237 (1970)CrossRefGoogle Scholar
  45. 45.
    P. M. Hinkle and J. F. Kirsch, Biochemistry, 10, 2717 (1971)CrossRefGoogle Scholar
  46. 46.
    P. Greenzaid and W. P. Jencks, Biochemistry, 10, 1210 (1971)CrossRefGoogle Scholar
  47. 47.
    P. M. Hinkle and J. F. Kirsch, Biochemistry, 9, 4633 (1970)CrossRefGoogle Scholar
  48. 48.
    P. M. Hinkle, Thesis, University of California (1970)Google Scholar
  49. 49.
    D. M. Chipman and N. Sharon, Z. Physiol. Chem, 165, 454 (1969)Google Scholar
  50. 50.
    C. Hansch, E. W. Deutsch, and R. N. Smith, J. Amer. Chem. Soc., 87, 2738 (1965)CrossRefGoogle Scholar
  51. 51.
    R. L. Nath and H. N. Rydon, Biochem. J., 57, 1 (1954)Google Scholar
  52. 52.
    A. N. Hall, S. Hollingshead, and H. N. Rydon, Biochem. J., 84, 390 (1962)Google Scholar
  53. 53.
    O. P. Malhotra and P. M. Dey, Biochem. J., 103, 739 (1967)Google Scholar
  54. 54.
    (a) B. Capon, Chem. Rev., 69,407 (1969); (b)D. C. Phillips, Prac. Nat. Acad. Sci. U.S.A., 57, 484 (1967); (c) E. Holler, J. A. Rupley, and G. P. Hess, Biochem. Biophys. Res. Comm., 37, 423 (1969); G. L. Rossi, E. Holler, S. Kumar, J. A. Rupley, and G. P. Hess, Biochem. Biophys. Res. Comm., 37, 757 (1969); I. Pecht, Y. I. Teichberg, and N. Sharon, FEBS Letters, 10, 241 (1970)Google Scholar
  55. 55.
    G. Lowe, G. Sheppard, M. L. Sinnott, and A. Williams, Biochem. J., 104, 893 (1967)Google Scholar
  56. 56.
    C. S. Tsai, J. Y. Tang, and S. C. Subbarao, Biochem. J., 114, 529 (1969)Google Scholar
  57. 57.
    T. Rand-Meir, F. W. Dahlquist, and M. A. Raftery, Biochemistry, 8, 4206 (1969)CrossRefGoogle Scholar
  58. 58.
    T. H. Fife and L. K. Jao, J. Amer. Chem. Soc., 90, 4081 (1968); T. H. Fife and L. H. Brod, J. Amer. Chem. Soc., 92, 1681 (1970)Google Scholar
  59. 59.
    L. N. Johnson, D. C. Phillips, and J. A. Rupley, Brookhaven Symp. Biol., 21, 120 (1969)Google Scholar
  60. 60.
    F. W. Dahlquist, T. Rand-Meir, and M. A. Raftery, Biochemistry, 8, 4214 (1969)CrossRefGoogle Scholar
  61. 61.
    Reference 34, p. 704Google Scholar
  62. 62.
    M. Caplow and W. P. Jencks, Biochemistry, 1, 883 (1962)CrossRefGoogle Scholar
  63. 63.
    D. M. Blow, J. J. Birktoft, and B. S. Hartley, Nature, 221, 337 (1969). References to the original suggestion are given in reference 62.Google Scholar
  64. 64.
    C. D. Hubbard and J. F. Kirsch, Federation Proc., 29, Abst. 3656 (1970), and in preparation.Google Scholar
  65. 65.
    M. L. Bender and K. Nakamura, J. Amer. Chem. Soc., 84, 2577 (1962)CrossRefGoogle Scholar
  66. 66.
    T. C. Bruice and S. J. Benkovic, J. Amer. Chem. Soc., 86,418 (1964); J. F. Kirsch and W. P. Jencks, J. Amer. Chem. Soc., 86, 837 (1964)CrossRefGoogle Scholar
  67. 67.
    J. Gerstein and W. P. Jencks, J. Amer. Chem. Soc., 86, 4655 (1964)CrossRefGoogle Scholar
  68. 68.
    A. Williams, Biochemistry, 9, 3383 (1970)CrossRefGoogle Scholar
  69. 69.
    Calculated from data given by E. L. Becker, Biochim. Biophys. Acta, 147, 289 (1967)Google Scholar
  70. 70.
    T. Inagami, S. S. York, and A. Patchornik, J. Amer. Chem. Soc., 87, 126 (1965)CrossRefGoogle Scholar
  71. 71.
    M. Caplow, J. Amer. Chem. Soc., 91, 3639 (1969); see also reference 43(a).Google Scholar
  72. 72.
    L. Parker and J. H. Wang, J. Biol. Chem., 243, 3729 (1968)Google Scholar
  73. 73.
    G. Lowe and A. Williams, Biochem. J., 96, 199 (1965)Google Scholar
  74. 74.
    J. F. Kirsch and M. Igelstrom, Biochemistry, 5, 783 (1966)CrossRefGoogle Scholar
  75. 75.
    G. Lowe and Y. Yuthavong, unpublished results quoted in reference 44.Google Scholar
  76. 76.
    K. B. Jacobson, J. Biol. Chem., 236, 343 (1961)Google Scholar
  77. 77.
    B. Riddle and W. P. Jencks, Biol. Chem., 246, 3250 (1971)Google Scholar
  78. 78.
    O. P. Malhotra and G. Philip, Biochem. Z., 346, 386 (1966)Google Scholar
  79. 79.
    J. K. Stoops, D. J. Horgan, M. T. C. Runnegar, J. de Jersey, E. C. Webb, and B. Zerner, Biochemistry, 8, 2026 (1969)Google Scholar
  80. 80.
    References cited in reference 46.Google Scholar
  81. 81.
    O. Gawron, C. J. Grelecki, and M. Duggan, Arch. Biochem. Biophys., 44, 455 (1953)CrossRefGoogle Scholar
  82. 82.
    G. D. Hegeman, E. Y. Rosenberg, and G. L. Kenyon, Biochemistry, 9, 4029 (1970)CrossRefGoogle Scholar
  83. 83.
    G. L. Kenyon and G. D. Hegeman, Biochemistry, 9, 4036 (1970)CrossRefGoogle Scholar
  84. 84.
    K. S. Dodgson, B. Spencer, and K. Williams, Biochem. J., 64, 216 (1956)Google Scholar
  85. 85.
    J. F. Koster and C. Veeger, Biochim. Biophys. Acta, 167, 48 (1968)Google Scholar
  86. 86.
    A. De Kok and C. Veeger, Biochim. Biophys. Acta, 167, 35 (1968)Google Scholar
  87. 87.
    A. H. Neims, D. C. De Luca, and L. Hellerman, Biochemistry, 5, 203 (1966). For further discussion related to the mechanism of action of D-amino acid oxidase see the article by A. H. Neims and L. Hellerman, Ann. Rev. Biochem., 39, 867 (1970)Google Scholar
  88. 88.
    R. A. Deitrich, L. Hellerman, and J. Wein, J. Biol. Chem., 237, 560 (1962)Google Scholar
  89. 89.
    C. H. Blomquist, Acta Chem. Scand., 20, 1747 (1966)CrossRefGoogle Scholar
  90. 90.
    B. Tabakoff and V. G. Erwin, J. Biol. Chem., 245, 3263 (1970)Google Scholar
  91. 91.
    H. W. Duckworth and J. E. Coleman, J. Biol. Chem., 245, 1613 (1970)Google Scholar
  92. 92.
    J. A. Mazrimas, P.-S. Song, L. L. Ingraham, and R. D. Draper, Arch. Biochem. Biophys., 100, 409 (1963)CrossRefGoogle Scholar
  93. 93.
    G. E. Lienhard, Biochemistry, 9, 3011 (1970)Google Scholar
  94. 94.
    S. Mahadevan and K. V. Thimann, Arch. Biochem. Biophys., 107, 62 (1964)CrossRefGoogle Scholar
  95. 95.
    D. Levine, T. W. Reid, and I. B. Wilson, Biochemistry, 8,2374 (1969); D. R. Trentham and H. Gutfreund, Biochem. J., 106, 455 (1968)Google Scholar
  96. 96.
    A. C. Henry and J. F. Kirsch, Biochemistry, 6, 3536 (1967)CrossRefGoogle Scholar
  97. 97.
    A. L. Fink and M. L. Bender, Biochemistry, 8, 5109 (1969) and references therein.Google Scholar
  98. 98.
    O. Viratelle, J. P. Tenu, J. Gamier, and J. Yon, Biochem. Biophys. Res. Comm., 37, 1036 (1969)Google Scholar
  99. 99.
    Reference 9, Chapter 2Google Scholar
  100. 100.
    T. H. Fife and J. B. Milstien, Biochemistry, 6, 2901 (1967); J. B. Milstien and T. H. Fife, Biochemistry, 8, 623 (1969)CrossRefGoogle Scholar
  101. 101.
    See reference 9, Chapter 3 for further discussion.Google Scholar
  102. 102.
    Reference 9, Chapter 4; J. H. Richards in The Enzymes, Vol. 2, p. 321, P. D. Boyer, ed. (Academic Press, New York, 3rd edn., 1970 )Google Scholar
  103. 103.
    P. W. Inward and W. P. Jencks, J. Biol. Chem., 240, 1986 (1965)Google Scholar

Copyright information

© Plenum Publishing Company Ltd. 1972

Authors and Affiliations

  • Jack F. Kirsch
    • 1
  1. 1.Department of BiochemistryUniversity of CaliforniaBerkeleyUSA

Personalised recommendations