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Catalysis by Chemically Modified CyD

For example, a superb mimic of the charge-relay system in serine proteases has been prepared by attaching both carboxylate and imidazole to a-, fi-, and y-CyDs [24]. The hydroxy group, the last component of the charge-relay system, is provided by the CyDs. The activity (kinetic parameters) of the -CyD-based artificial enzyme for ester hydrolysis is close to that of a hymotrypsin. These artificial enzymes show acylation, deacylation, and turnover, as is observed in the reactions of chymo-trypsin. The substrate-specificity is dependent on the kind of CyD used, since it is primarily governed by the substrate-binding process. In phenyl ester hydrolysis, a- and yS-CyD-based artificial enzymes are better than the y-CyD-based artificial enzyme. For the hydrolysis of tryptophan ethyl ester, however, the y-CyD-based artificial enzyme is the best. In another serine protease model, tripeptide (Ser-His-Asp) is directly introduced to the primary hydroxyl side of f -CyD [25]. This [Pg.101]

In principle, appropriate artificial enzymes for any target reaction should be obtained when the corresponding catalyst is covalently bound to CyDs. The validity of this idea has been substantiated in various examples, making this a quite important field. However, there are many review artides that deal with these subjects, and thus they are only briefly described here to avoid urmecessary repetition [28]. [Pg.102]


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