Functional mimicry of the active site of carboxypeptidase A by a molecular imprinting strategy: cooperativity of an amidinium and a copper ion in a transition-state …
J Liu, G Wulff
Index: Liu, Jun-Qiu; Wulff, Guenter Journal of the American Chemical Society, 2004 , vol. 126, # 24 p. 7452 - 7453
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Citation Number: 115
Abstract
A model for the natural enzyme carboxypeptidase A was prepared by molecular imprinting in synthetic polymers. An unusually high activity and efficiency for carbonate hydrolysis could be obtained by imprinting with a stable transition-state analogue template and introducing an amidinium group and a Cu2+ ion-binding site in a defined orientation to each other into the active site. With substrates having a very similar structure to the template, ...
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