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

By Istvan T. Horvath ed.-in-chief

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Fierke, E. J. Toone, and J. H. Naismith, Directed evolution of a new catalytic site in 2-keto-3-deoxy-6phosphogluconate aldolase from Escherichia coli, Structure 2001, 9, 1–10. A. Zaks, Industrial biocatalysis, Curr. Opin. Chem. Biol. 2001, 5, 130–136. 19 2 Characterization of a (Bio-)catalyst Summary Enzymes are a class of macromolecules with the ability both to bind small molecules and to effect reaction. Stabilizing forces such as hydrophobic effects only slightly dominate destabilizing forces such as Coulombic forces of equal polarity; thus the Gibbs free enthalpy of formation of proteins, ∆Gformation, is only weakly negative.

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Biol. Chem. 1969, 244, 6049–6055. 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.

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