Elliott & Elliott: Biochemistry and Molecular Biology 4e
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Steitz, T. A., Shoham, M., and Bennett, W. S. (1981). Structural dynamics of yeast hexokinase during catalysis. Phil. Trans. Roy Soc of the Lond serB bio sc, 293, 43-52 [DOI: 10.1098/rstb.1981.0058].
Discusses the conformational change of the enzyme on binding of glucose.
Srere, P. A. (1984). Why are enzymes so big? Trends Biochem. Sci., 9, 387-90 [DOI: 10.1016/0968-0004(84)90221-4].
A necessarily speculative, but interesting article
Koshland, D. E. (1987). Evolution of catalytic function. Cold Spring Harbor Symp. Quant. Biol., LII, 1-7.
A concise clear summary of the basic roles of active sites and of enzyme conformational change in catalysis.
Kraut, J. (1988). How do enzymes work? Science, 242, 533-40 [DOI: 10.1126/science.3051385] [PubMed: 3051385].
Enzyme catalysis explained by the principle of transition state stabilization. Also describes catalytic antibodies specific for transition state analogues.
Schramm, V. L. (1998). Enzymatic transition state analog design. Annu. Rev. Biochem., 67, 693-720 [DOI: 10.1146/annurev.biochem.67.1.693].
Blow, D. M. (1997). The tortuous story of Asp? His? Ser: structural analysis of a-chymotrypsin. Trends Biochem. Sci., 22, 405-8 [DOI: 10.1016/S0968-0004(97)01115-8].
A personal story of how the classical elucidation of the mechanism of this enzyme took place.
Dodson, G. and Wlodawer, A. (1998). Catalytic triads and their relatives. Trends Biochem. Sci., 23, 347-52 [DOI: 10.1016/S0968-0004(98)01254-7].
A review of the mechanism of chymotrypsin catalysis together with a discussion of other enzymes using the ?serine? catalytic triad and their evolutionary relationships.
Hooper, N. M. (ed.). (2002). Proteases in biology and medicine. Essays Biochem., 36, 1-167.
A complete issue with 12 reviews on many aspects of proteases, including caspases, cancer, proteasomes, and blood clotting.