Biocatalytic with other enzymes

Biocatalytic Asymmetric Oxidations with Other Enzymes... 

In recent years biotransformations have also shown their potential when applied to nucleoside chemistry [7]. This chapter will give several examples that cover the different possibiUties using biocatalysts, especially lipases, in order to synthesize new nucleoside analogs. The chapter will demonstrate some applications of enzymatic acylations and alkoxycarbonylations for the synthesis of new analogs. The utQity of these biocatalytic reactions for selective transformations in nucleosides is noteworthy. In addition, some of these biocatalytic processes can be used not only for protection or activation of hydroxyl groups, but also for enzymatic resolution of racemic mixtures of nucleosides. Moreover, some possibilities with other biocatalysts that can modify bases, such as deaminases [8] or enzymes that catalyze the synthesis of new nucleoside analogs via transglycosylation [9] are also discussed. 

Electroanalyhcal techniques (also in combination with other techniques, e.g., ophcal techniques such as photometry and Raman spectrometry) can be employed to inveshgate many functional aspects of proteins and enzymes in particular. It is possible to study the biocatalytic process with respect to the chemistry of the active site, the interfacial and intramolecular ET, slow enzyme achva-tors or inhibitors, the pH dependence, the transport of tlie substrate, and even more parameters. For example, slow scan voltammetry can be used to determine the relation of ET rates or of protonation and ligand binding. In contrast, fast scan voltammetry allows the determination of rates of interfacial ET. In addition, it is also possible to investigate chemical reactions that are coupled to the ET process, such as protonation. The use of direct ET for mechanistic studies of redox enzymes was recently reviewed by Leger and Bertrand [27]. Mathemahcal models help to elucidate the impact of different variables on the enhre current signal [27, 75, 76]. 

The results of investigations of enzymatic activity in the immobilized state. When laccase, peroxidase, and other enzymes are adsorbed on dispersive electroconductive carriers, their enzymatic activity perceptibly declines, thus indicating a denaturing of part of the macromolecules. In this case, however, there is a sufficient quantity of denatured enzyme molecules strongly bonded with the carrier, which display a specific biocatalytic activity in model reactions of the substrates. It is these molecules of the enzyme, as will be seen further, that are responsible also for the electrocatalytic activity of the system. 

Sequential biocatalytic cascade reactions are characterized by the use of multiple enzymatic steps involving various biocatalysts. One cascade reaction can consist of an enzyme-module with several enzymes if substrate and inhibitor kinetics are compatible with these combinations. Sequential use of such enzyme-modules surpassing the work-up of intermediate products is the criterion for the idea of cascade reactions we address here on the one hand, the synthesis of nucleotide sugars and their derivatives, on the other hand, the synthesis of glycan epitopes with multiple GTs. 

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