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Selective substrate binding

The considerable interest in the design of container molecules [26, 27, 30], for their potential application as nano-scale chemical reactors has particularly received much attention [97]. In this sense, supramolecular catalysis allowing the chemical transformation of a substrate selectively entrapped within a molecular receptor, will behave as a chemical reactor [98]. One way to obtain a supramolecular catalysis, is to design a molecular receptor containing a lipophilic cavity allowing selective substrate binding, and specific sites for metal ion coordination [97, 99]. Attempts in this direction have... [Pg.84]

These examples clearly demonstrate that well-defined geometries, with asymmetric environments around the active site, can be generated. Comfenation of the experimental information summarized here with the extensive knowledge currently available on synthetic receptors for selective substrate binding, opens intriguing possibilities for the design of sophisticated supramolecular catalysts. [Pg.188]

Smith PA, Sorich M, McKinnon R, Miners JO. QSAR and pharmacophore modelling approaches for the prediction of UDP-glucuronosyltransferase substrate selectivity and binding. Pharmacologist 2002 44 supplement. [Pg.462]

The three-dimensional X-ray structure of the enzyme [19] reveals that several Thr residues occur in both the NADH cofactor and substrate binding sites (Fig. 21.5 A see p. 463). A Met residue (Metl7) is also present at the interface between the cofactor NADH and a substrate analog pyridine-2,6-dicarboxylate (PDC) (Fig. 21.5 A). Therefore, we prepared a sample of DHPR that was selectively labeled in these amino acid residues as follows 13C /1H Met, 13C /1H lie, 13C/1H Thr and uniformly 2H-labeled elsewhere ([MIT]-DHPR). This labeling can be achieved by supplementing the media with appropriate commercially available labeled amino acids, 12C/2H-labeled glucose and DzO [20] (see also the caption to Fig. 21.5 for details). [Pg.464]


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