Summary and Bibliography of Chapter 1

1. Enzymes are specific catalysts of vast range and utility.
2. Their activity is governed by their structure and physical environment.
3. Care should be taken over the interpretation of reported units of enzymic activity and the conditions necessary for maximum productivity.
4. Enzymes may lose their catalytic activity reversibly or irreversibly due to denaturation or inhibition, dependent upon the conditions
5. The values of the K_m, V_max, specificity constants, pH_optimum and rate of thermal denaturation are all of relevance and utility to enzyme technology
   

References and Bibliography

1. Bender, M.L., Kezdy, J.F. & Gunter, C.R. (1964). The anatomy of an enzymatic catalysis: a-Chymotrypsin. Journal of the American Chemical Society, 86, 3714-21.
2. Chaplin, M.F. (1986). Protein structure and enzyme activity. Oxford, UK: IRL Press Ltd. (This is a CAL/simulation software package suitable for IBM or BBC micocomputers)
3. Cornish-Bowden, A. (1974). A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochemical Journal, 137, 143-4. 
4. Cornish-Bowden, A. (1976). Principles of enzyme kinetics. London: Butterworth.
5. Cornish-Bowden, A. & Endrenyi, L. (1986). Robust regression of enzyme kinetic data. Biochemical Journal, 234, 21-9. 
6. Cornish-Bowden, A., Porter, W.R. & Trager, W.F. (1978). Evaluation of distribution-free confidence limits for enzyme kinetic parameters. Journal of Theoretical Biology, 74, 163-75. 
7. Crompton, I.E. & Waley, S.G. (1986). The determination of specificity constants in enzyme-catalysed reactions. Biochemical Journal, 239, 221-4.Eisenthal, R. & Cornish-Bowden, A. (1974). The direct linear plot. Biochemical Journal, 139, 715-20. 
8. Fersht, A. (1985). Enzyme structure and mechanism, 2nd edn, New York: W.H.Freeman & Co.Henderson, P.J.F. (1978). Statistical analysis of enzyme kinetic data. Techniques in the life sciences, Biochemistry vol. B1/11, Techniques in protein and enzyme biochemistry - part 2. pp B113/1-41, Amsterdam: Elsevier/North-Holland Biomedical Press. 
9. Henley, J.P. & Sadana, A. (1985). Categorization of enzyme deactivations using a series-type mechanism. Enzyme and Microbial Technology, 7, 50-60.
10. Hill, C.M., Waight R.D. & Bardsley, W.G. (1977). Does any enzyme follow the Michaelis-Menten equation? Molecular and Cellullar Biochemistry, 15, 173-8. 
11. Koshland, D.E. Jr. (1962). The comparison of non-enzymic and enzymic reaction velocities. Journal of Theoretical Biology, 2, 75-86. 
12. Michaelis, L. & Menten, M.L. (1913). The kinetics of invertin action. Biochemische Zeitschrift, 49, 333-69.