A Macrocyclic Enzyme Model System. Substrate Specificity for the Inclusion into Paracyclophane Oxime and the Subsequent Acyl Transfer Reaction
Author:
Publisher
The Chemical Society of Japan
Subject
General Chemistry
Link
https://www.jstage.jst.go.jp/article/bcsj1926/48/5/48_5_1537/_pdf
Reference19 articles.
1. Catalytic Accelerations of 1012-Fold by an Enzyme-Like Synthetic Polymer
2. Imidazole catalyses in aqueous systems. V. Enzyme-like catalysis in the hydrolysis of a phenyl ester by copolymers containing a benzimidazole group. Rate acceleration by bound phenols and the mode of side chain aggregation in polymer catalysts
3. Nucleophilic and metal ion acceleration of ester hydrolysis in a hydrophobic complex. Reactive enzyme model system
4. A Macrocyclic Enzyme Model System. Acyl Transfer fromp-Nitrophenyl Carboxylates to Paracyclophane Oxime
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3. Design, Synthesis, and Molecular Recognition Function of Water-Soluble Cyclophanes Having Hydrophobic Cavities;YAKUGAKU ZASSHI;1988
4. The effect of hydrophobic-lipophilic interactions on chemical reactivity. 10. The competition between the aggregation of long-chain esters and the formation of inclusion complexes of these esters with amylose;Proceedings / Indian Academy of Sciences;1987-06
5. The effect of hydrophobic-lipophilic interactions on chemical reactivity: 7. Fourteen and eighteen-membered-ring neighboring group participations;Acta Chimica Sinica;1987-02
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