By Istvan T. Horvath ed.-in-chief

ISBN-10: 0471138223

ISBN-13: 9780471138228

ISBN-10: 0471241830

ISBN-13: 9780471241836

ISBN-10: 0471979015

ISBN-13: 9780471979012

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By utilizing the thermodynamic cycle the quotient of the constants of formation of the transition state Ke≠/Ku≠ can be equated with the quotient of the dissociation constants for substrate KS and transition state KT [Eq. 7)]. 7) Although only a few data are available for the comparison of κe · νe, and κu · νu, it is assumed that the two terms do not differ much in magnitude, so that Eq. 8) holds approximately. 8) This is the equation derived by Kurz, expressed here for the case of an enzyme reaction.

1 Chronology of the Most Important Theories of Enzyme Activity Just one year after Ostwald’s hypothesis about the existence of catalysts in 1893, when nobody yet had a clear idea of the structure and composition of enzymes, Emil Fischer voiced the idea for the first time that a substrate molecule fits into the pocket of an enzyme, the “lock-and-key hypothesis” (Fischer, 1894). Both the lock (enzyme) as well as the key (substrate) were regarded as rigid. This hypothesis was modified later in many ways.

The dimensions of merit important for determining, evaluating, or optimizing a process are (i) product yield, (ii) (bio)catalyst productivity, (iii) (bio)catalyst stability, and (iv) reactor productivity. The pertinent quantities are turnover number (TON) (= [S]/[E]) for (ii), total turnover number (TTN) (= mole product/mole catalyst) for (iii) and space–time yield [kg (L · d)–1] for iv). e. y. 1 kg (L · d)–1. 1 Basis of the Activity of Enzymes: What is Enzyme Catalysis? Enzymes are a class of multifunctional, multivalent macromolecules with the ability to bind small molecules and, much more importantly, subsequently to effect reaction.

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

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