Biochemistry pp 83-116 | Cite as


  • J. Stenesh


Enzymes are the catalysts of biochemical reactions. They serve to make reactions in living systems proceed at accelerated rates. Without the action of enzymes, reactions would proceed too slowly, and life, as we know it, would not be feasible.


Enzyme Commission Turnover Number Tetrahedral Intermediate Allosteric Effector Allosteric Enzyme 
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.


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Selected Readings

  1. Carreras, W., and Santi, D. V., The catalytic mechanism and structure of thymidylate synthase, Annu. Rev. Biochem. 64: 721–762 (1995).PubMedCrossRefGoogle Scholar
  2. Carter, P., and Wells, J. A., Dissecting the catalytic triad of a serine protease, Nature (London) 332: 564–568 (1988).CrossRefGoogle Scholar
  3. Fersht, A. R., and Gani, D. (eds.), Enzymic Catalysis, Cambridge University Press, Cambridge (1991).Google Scholar
  4. Kim, Y., Eom, S. H., Wang, J., Lee, D. S., Suh, S. W., and Steltz, T. A., Crystal structure of Thermus aquaticus DNA polymerase, Nature (London) 376: 612–616 (1995).CrossRefGoogle Scholar
  5. Koleske, A. J., and Young, R. A., An RNA polymerase II holoenzyme responsive to activators, Nature (London) 368: 466–469 (1994).CrossRefGoogle Scholar
  6. Koshland, D. E., Correlation of structure and function of enzyme action, Science 142: 1533–1541 (1963).PubMedCrossRefGoogle Scholar
  7. Liu, Y., Van Heeswijck, R., Hoj, P., and Hoogenraad, N., Purification and characterization of ornithine acetyltransferase from Saccharomyces cerevisiae, Eur. J. Biochem. 228: 291–296 (1995).PubMedCrossRefGoogle Scholar
  8. Lohse, P. A., and Szostak, J. W., Ribozyme-catalyzed amino acid transfer reactions, Nature (London) 381: 442–444 (1996).CrossRefGoogle Scholar
  9. Matthews, J. C., Fundamentals of Receptor, Enzyme, and Transport Kinetics, CRC Press, Boca Raton, Florida (1993).Google Scholar
  10. Monod, J., Changeux, J.-P., and Jacob, F., Allosteric proteins and cellular control systems, J. Mol. Biol. 6: 306–329 (1963).PubMedCrossRefGoogle Scholar
  11. Pinot, F., et al.,Molecular and biochemical evidence for the involvement of the Asp-333 His-523 pair in the catalytic mechanism of soluble epoxide hydrolase, J. Biol. Chem. 270:7968–7987 (1995).Google Scholar
  12. Xue, Q., and Yeung, E. S., Differences in the chemical reactivity of individual molecules of an enzyme, Nature (London) 373: 681–683 (1995).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • J. Stenesh
    • 1
  1. 1.Western Michigan UniversityKalamazooUSA

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