So do we understand how enzymes work?

Structure

Volumn 8, Issue 4, 2000, Pages

  Blow, David ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN A; TRYPSIN; TRYPSIN INHIBITOR;

CATALYSIS; ENERGY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME STRUCTURE; ENZYMOLOGY; HYDROLYSIS; PRIORITY JOURNAL; SHORT SURVEY; THERMODYNAMICS;

EID: 0034656302     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00125-8     Document Type: Review

References (35)

1. Willstätter R. Problems and Methods in Enzyme Research. 1927;Cornell University Press, Ithaca.
2. Haldane J.B.S. Enzymes. 1930;Longmans Green, London, UK.
3. Mirsky A., Pauling L. On the structure of native, denatured and coagulated protein. Proc. Natl Acad. Sci. USA. 22:1936;439-447.
4. Pauling L. Molecular architecture and biological reactions. Chem. Eng. News. 24:1946;1375-1377.
5. Blake C.C.F., Phillips D.C.et al. Structure of hen egg-white lysozyme - a three-dimensional Fourier synthesis at 2 Å resolution. Nature. 206:1965;757-761.
6. Blow D.M. The tortuous story of Asp.His.Ser: structural analysis of α-chymotrypsin. Trends Biochem. Sci. 22:1997;405-408.
7. Matthews B.W., Sigler P.B., Henderson R., Blow D.M. Three-dimensional structure of tosyl α-chymotrypsin. Nature. 214:1967;652-656.
8. Wright C.S., Alden R.A., Kraut J. Structure of subtilisin BPN′ at 2.5 Å resolution. Nature. 221:1969;235-242.
9. Blow D.M., Birktoft J.J., Hartley B.S. Role of a buried acid group in the mechanism of action of chymotrypsin. Nature. 221:1969;337-340.
10. Blow D.M. Structure and mechanism of chymotrypsin. Accts. Chem. Res. 9:1976;145-152.
11. Rühlmann A., Kukla D., Schwager P., Bartels K., Huber R. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. J. Mol. Biol. 77:1973;417-436.
12. Sweet R.M., Wright H.T., Janin J., Chothia C.H., Blow D.M. Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6 Å resolution. Biochemistry. 13:1974;4212-4228.
13. Henderson R. Catalytic activity of α-chymotrypsin in which histidine-57 has been methylated. Biochem. J. 124:1971;13-18.
14. Wright C.S., Hess G.P., Blow D.M. Structure of crystalline methyl-chymotrypsin. J. Mol. Biol. 63:1972;295-303.
15. Craik C.S., Roczniak S., Largman C., Rutter W.J. The catalytic role of the active site aspartic acid in serine proteases. Science. 237:1987;909-913.
16. Freer S.T., Kraut J., Robertus J.D., Wright H.T., Xuong N.H. Chymotrypsinogen: 2.5 Å crystal structure, comparison with α-chymotrypsin, and implications for zymogen activation. Biochemistry. 9:1970;1997-2009.
17. Kraut J. Serine proteases: structure and mechanism of catalysis. Annu. Rev. Biochem. 46:1977;331-358.
18. Fersht A.R. Enzyme Structure and Mechanism Chapter 7B. 1977;Freeman, Reading, UK.
19. Hayashi Y., Lawson W.B. Stereochemistry of the active site of α-chymotrypsin; binding geometry of tryptophan derivatives. J. Biol. Chem. 244:1969;4158-4167.
20. Rodgers P.S., Goaman L.C.G., Blow D.M. On the correlation between three-dimensional structure and reactivity for a series of locked substrates of chymotrypsin. J. Am. Chem. Soc. 98:1976;6690-6695.
21. Storm D.R., Koshland D.E. Jr. A source for the special catalytic power of enzymes. Proc. Natl Acad. Sci. USA. 66:1970;445-452.
22. Page M.I., Jencks W.P. Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect. Proc. Natl Acad. Sci. USA. 68:1971;1678-1683.
23. Jencks W.P. From chemistry to biochemistry to catalysis to movement. Annu. Rev. Biochem. 66:1997;1-18.
24. Fersht A.R. Structure and Mechanism in Protein Science. 1999;Freeman, New York.
25. Jencks W.P. Catalysis in Chemistry and Enzymology. 1969;McGraw Hill, London, UK.
26. Jencks W.P. Foreword. Catalysis in Chemistry and Enzymology Enlarged edition. 1977.
27. Lehninger, A.L., Nelson, D.L. & Cox, M.M. (1993). Principles of Biochemistry. 2nd Edition, p. 225, Worth, New York.
28. Stryer, L. (1995). Biochemistry. 4th Edition, pp. 200-201, Freeman, New York.
29. Matthews, C.K. & van Holde, K.E. (1996). Biochemistry. 2nd Edition, pp. 368-369, Benjamin/Cummings, Wokingham, UK.
30. Voet, D. & Voet, J.G. (1995). Biochemistry. 2nd Edition, p. 379, Wiley, Chichester, UK.
31. Jencks W.P. Binding energy, specificity, and enzymic catalysis: the Circe effect. Adv. Enzymol. 43:1975;219-410.
32. Warshel A. Computer Modelling of Chemical Reactions in Enzymes. 1991;Wiley, Chichester, UK.
33. Náray-Szabó G., Warshel A. Computational Approaches to Biochemical Reactivity. 1997;Kluwer, Dordrecht, Netherlands.
34. Smart O.S. A new method to calculate reaction paths for conformational transitions of large molecules. Chem. Phys. Lett. 222:1994;503-512.
35. Editorial. (1999). Can physics deliver another biological revolution? Nature 397, 89.