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Biocatalysis 2004 Bommanus Riebel by Istvan T. Horvath ed.-in-chief

By Istvan T. Horvath ed.-in-chief

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F. M. Menger, Enzyme reactivity from an organic perspective, Acc. Chem. Res. 1993, 26, 206–212. G. P. Moss, Enzyme Nomenclature, Academic Press, San Diego, CA, 1992, and later Supplements. H. Oikawa, K. Katayama, Y. Suzuki, and A. Ichihara, Enzymic activity catalyzing exo-selective Diels–Alder reaction in solanapyrone biosynthesis, J. Chem. , Chem. Commun. 1995, 1321–1322. J. L. Pawlak, R. E. Padykula, J. D. Kronis, R. A. Aleksejczyk, and G. A. Berchtold, Structural requirements for catalysis by chorismate mutase, J.

Even the triple mutant without any amino acid from the original catalytic center displayed a 1000-fold higher reaction rate than the uncatalyzed reaction, and the remainder of the enzyme molecule bound the substrate better in the transition state than in the ground state (Carter, 1988). y The numerous interactions between enzyme side chains and substrate molecules act synergistically, so the fit is quite exact. This cooperativity enhances substrate specificity, for a small change of substrate can effect a large change in the binding of the transition state.

Commun. 1995, 1321–1322. J. L. Pawlak, R. E. Padykula, J. D. Kronis, R. A. Aleksejczyk, and G. A. Berchtold, Structural requirements for catalysis by chorismate mutase, J. Am. Chem. Soc. 1989, 111, 3374–3381. W. J. Quax, N. T. Mrabet, R. G. M. Luiten, P. W. Schuurhuizen, P. Stanssens, and I. Lasters, Enhancing the thermostability of glucose isomerase by protein engineering, Bio/Technology 1991, 9, 738−742. J. P. Rasor and E. Voss, Enzyme-catalyzed processes in pharmaceutical industry, Appl. Catal.

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