Artificial enzymes: synthesis of imidazole substituted at C(2) of β-cyclodextrin as an efficient enzyme model of chymotrypsin
- 1 January 1990
- journal article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Chemical Communications
- No. 1,p. 10-11
- https://doi.org/10.1039/c39900000010
Abstract
Imidazole has been attached at C(2) on the more open face of β-cyclodextrin to mimic the enzyme chymotrypsin; this chemical model is shown to be catalytically far superior to that with an imidazole on the primary side [C(6)] of cyclodextrin.Keywords
This publication has 9 references indexed in Scilit:
- Mimics of transaminase enzymesJournal of the American Chemical Society, 1986
- Functionalized cyclodextrins as holoenzyme mimics of thiamine-dependent enzymesBioorganic Chemistry, 1984
- Cyclodextrin catalysis as a model for enzyme actionAccounts of Chemical Research, 1982
- Selective sulfonation of a secondary hydroxyl group of β-cyclodextrinTetrahedron Letters, 1982
- The first successful carbonic anhydrase model prepared through a new route to regiospecifically bifunctionalized cyclodextrinJournal of the American Chemical Society, 1980
- Synthesis of 2-amino-2-deoxy-D-[1-13C]glucose and 2-amino-2-deoxy-D-[1-13C]mannoseCarbohydrate Research, 1978
- Cyclodextrin ChemistryPublished by Springer Nature ,1978
- A study of 13CH coupling constants in hexopyranosesJournal of the Chemical Society, Perkin Transactions 2, 1974
- Carbon-13 magnetic resonance. XVII. Pyrimidine and purine nucleosidesJournal of the American Chemical Society, 1970