Enzyme-like catalytic activity

Evolution of Synthetic Polymers with Enzyme-like Catalytic Activities... 

An edited volume entitled Molecular Movements and Chemical Reactivity as Conditioned by Membranes, Enzymes, and Other Macromolecules includes sections on synzymes (synthetic polymers with enzyme-like catalytic activities), diffusion-reaction in structured media and membranes bearing enzymes, and structures and energetics of proteins and their active sites. ... 

Klotz, l.M. and Suh, J., Evolution of synthetic polymers with enzyme-like catalytic activities. In Breslow, R. (Ed.), Artificial Enzymes, Wiley-VCH, Weinheim, Germany, 2005, pp. 63-88. 

In general, mutation of the nucleophilic carhoxylate to an inert residue (Ala, Gly, etc.) leaves an enzyme without catalytic activity. Apparent residual activities are likely arise from wild-type contamination or catalytic rescue by added salts. 

In contrast to the situation in the absence of catalytically active Lewis acids, micelles of Cu(DS)2 induce rate enhancements up to a factor 1.8710 compared to the uncatalysed reaction in acetonitrile. These enzyme-like accelerations result from a very efficient complexation of the dienophile to the catalytically active copper ions, both species being concentrated at the micellar surface. Moreover, the higher affinity of 5.2 for Cu(DS)2 compared to SDS and CTAB (Psj = 96 versus 61 and 68, respectively) will diminish the inhibitory effect due to spatial separation of 5.1 and 5.2 as observed for SDS and CTAB. 

The first hint that two active-site carboxyl groups—one proto-nated and one ionized—might be involved in the catalytic activity of the aspartic proteases came from studies of the pH dependence of enzymatic activity. If an ionizable group in an enzyme active site is essential for activity, a plot of enzyme activity versus pH may look like one of the plots at right. 

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