A novel cyclodextrin homodimer with dual-mode substrate binding and esterase activity

Date

2000-06-20

Author

Tastan, P
Akkaya, EU

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A novel cyclodextrin homodimer with two beta-cyclodextrin units tethered from the primary side by a tris(2-aminoethyl)amine linker was found to be hydrolytically active. The hydrolysis of a ditopic activated carbonate ester was accelerated 150-fold and a Lineweaver-Burk plot showed a biphasic curve indicative of two different binding modes for the activated carbonate ester.

Subject Keywords

Enzyme models, Enzyme mimics, Artificial enzymes, Cyclodextrins

URI

https://hdl.handle.net/11511/66129

Journal

JOURNAL OF MOLECULAR CATALYSIS A-CHEMICAL

DOI

https://doi.org/10.1016/s1381-1169(00)00159-x

Collections

Department of Chemistry, Article

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Citation Formats

P. Tastan and E. Akkaya, “A novel cyclodextrin homodimer with dual-mode substrate binding and esterase activity,” JOURNAL OF MOLECULAR CATALYSIS A-CHEMICAL, pp. 261–263, 2000, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/66129.