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A novel cyclodextrin homodimer with dual-mode substrate binding and esterase activity
Date
2000-06-20
Author
Tastan, P
Akkaya, EU
Metadata
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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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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.