BIBLIOGRAPHY

Books

Copeland, R. A., Enzymes: A Practical Introduction to Structure, Mechanism, andData Analysis, 2nd edition, Wiley-VCH, New York, 1999.

Cook, P. F., Steady-State Enzyme Kinetics, Oxford University Press, New York,1997.

Cornish-Bowden, A., Principles of Enzyme Kinetics, Butterworth, London, 1979.Cornish-Bowden, A., Analysis of Enzyme Kinetic Data, Oxford University Press,

Oxford, 1995.Cornish-Bowden, A., Fundamentals of Enzyme Kinetics, Portland Press, London,

1995.Cornish-Bowden, A., and C. W. Wharton, Enzyme Kinetics, IRL Press, Oxford,

1988.Dixon, M. C., and E. C. Webb, Enzymes, 3rd edition, Academic Press, San Diego,

CA, 1979.Fersht, A., Enzyme Structure and Mechanism, W. H. Freeman, New York, 1977.Fersht, A., Enzyme Structure and Mechanism, 2nd edition, W. H. Freeman, New

York, 1985.Fersht, A., Structure and Mechanism in Protein Science: A Guide to Enzyme

Catalysis and Protein Folding, W.H. Freeman, New York,1999.Fromm, H., Initial Rate Enzyme Kinetics, Springer-Verlag, New York, 1975.Gutfreund, H., Enzymes: Physical Principles, Wiley-Interscience, London, 1972.Jencks, W. P., Catalysis in Chemistry and Enzymology, Dover Publications, New

York, 1987.

217

Enzyme Kinetics: A Modern Approach. Alejandro G. MarangoniCopyright 2003 John Wiley & Sons, Inc.

ISBN: 0-471-15985-9

218 BIBLIOGRAPHY

Piszkiewicz, D., Kinetics of Chemical and Enzyme-Catalyzed Reactions, OxfordUniversity Press, New York, 1977.

Plowman, K. M., Enzyme Kinetics, McGraw-Hill, New York, 1972.Purich, D. L., Ed., Enzyme Kinetics and Mechanism Part D, Developments in

Enzyme Dynamics, Methods in Enzymology, Vol. 249, Academic Press, SanDiego, CA, 1995.

Purich, D. L., and R. D. Allison, Handbook of Biochemical Kinetics, AcademicPress, San Diego CA, 1999.

Schulz, A. R., Enzyme Kinetics, Cambridge University Press, Cambridge, 1994.Segel, I. H., Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and

Steady-State Enzyme Systems, John Wiley and Sons, New York, 1975.Segel, I. H., Biochemical Calculations: How to Solve Mathematical Problems in

General Biochemistry, 2nd edition, John Wiley and Sons, New York, 1976.Silverman, R. B., Mechanism-Based Enzyme Inactivation: Chemistry and

Enzymology, Vol I and II, CRC Press, Boca Raton, FL, 1988.Walsh, C. T., Enzymatic Reaction Mechanisms, W.H. Freeman, New York, 1979.

Selection of Classic Papers

Cleland, W. W., 1963, The kinetics of enzyme-catalyzed reactions with two ormore substrates or products. I. Nomenclature and rate equations. II. Inhibition:nomenclature and theory. III. Prediction of initial velocity and inhibition byinspection, Biochem. Biophys. Acta 67: 104–137, 173–187, 188–196.

Cleland, W. W., 1977, Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies, Adv. Enzymol. 45: 273–387.

Cleland, W. W., 1979, Statistical analysis of enzyme kinetic data, MethodsEnzymol. 63: 103–138.

Cleland, W. W., 1987, The use of isotope effects in the detailed analysis ofcatalytic mechanisms of enzymes, Bioorg. Chem. 15: 283–302.

Duggleby, R. G., 1994. Analysis of progress curves for enzyme-catalyzedreactions: application to unstable enzymes, coupled reactions and transient-state kinetics, Biochim. Biophys. Acta 1205: 268–274.

Fromm, H. J., 1979. Use of competitive inhibitors to study substrate bindingorder, Methods. Enzymol. 63: 467–486.

Gerlt, J. A., and J. W. Kozarich, 1991, Electrophilic catalysis can explain theunexpected acidity of carbon acids in enzyme catalyzed reactions, J. Amer.Chem. Soc. 113: 9667–9669.

Hill, A. V., 1913. The combinations of haemoglobin with oxygen and withcarbon dioxide, Biochem. J. 7: 471–480.

Knowles, J. R., and J. Albery, 1977, Perfection in enzyme catalysis: theenergetics of triosephosphate isomerase, Acc. Chem. Res. 10: 105–111.

BIBLIOGRAPHY 219

Koshland, D. E., Jr. and K. E.Neet, 1968, The catalytic and regulatory propertiesof enzymes, Annu. Rev. Biochem. 37: 359–410.

Koshland, D. E., Jr., G. Nemethy, and D. Filmer, 1966, Comparison ofexperimental binding data and theoretical models in proteins containingsubunits, Biochemistry 5: 365–385.

Kraut, J., 1988, How do enzymes work? Science 242: 533–540.Mesecar, A. D., and D. E. Koshland, 2000, A new model for protein

stereospecificity, Nature 403: 614–615.Mesecar, A. D., B. L. Stoddard and D. E. Koshland, 1997, Orbital steering in

the catalytic power of enzymes: small structural changes with large catalyticconsequences, Science 277: 202–206.

Michaelis, L., and M. L. Menten. 1913, Die Kinetik der Invertinwirkung,Biochem. Z. 49: 333–369.

Monod, J., J. P. Changeux and F. Jacob, 1963, Allosteric proteins and cellularcontrol systems, J. Mol. Biol. 6: 306–329.

Monod, J., J. Wyman, and J. P. Changeux, 1965, On the nature of allosterictransitions: a plausible model. J. Mol. Biol. 12: 88–118.

Morrison, J. F., and C. T. Walsh, 1988, The behavior and significance of slowbinding enzyme inhibitors, Adv. Enzymol. 61: 201–301.

Page, M. I., and W. P. Jencks, 1971, Entropic contributions to rate enhancement,Proc. Natl. Acad. Sci. USA 68: 1678.

Radzicka, A., and R. Wolfenden, 1995, A proficient enzyme, Science 267: 90–93.Rudolph, F. B., 1979, Product inhibition and abortive complex formation,

Methods Enzymol. 63: 411–436.Schramm, V. L., 1998, Enzymatic transition states and transition state analog

design, Annu. Rev. Biochem. 67: 693–720.