Isolation of DNA Aptamers for CDP-Ribitol Synthase, and Characterization of Their Inhibitory and Structural Properties

Two birds with one stone: Four DNA aptamers were isolated for Bcs1, a bifunctional enzyme that catalyzes both the reduction of ribulose 5‐phosphate by using NADPH and cytidylyltransfer by using CTP. The inhibitory effects of these aptamers towards Bcs1 and their secondary structural properties were...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2007-11, Vol.8 (17), p.2052-2057
Main Authors: Allali-Hassani, Abdellah, Pereira, Mark P, Navani, Naveen K, Brown, Eric D, Li, Yingfu
Format: Article
Language:English
Subjects:
aptamers
Aptamers, Nucleotide - chemistry
Aptamers, Nucleotide - genetics
Aptamers, Nucleotide - isolation & purification
Aptamers, Nucleotide - metabolism
CDP-ribitol synthase
enzyme catalysis
inhibitors
Inhibitory Concentration 50
Molecular Sequence Data
Molecular Structure
Mutation - genetics
Nucleoside Diphosphate Sugars - chemistry
Nucleoside Diphosphate Sugars - genetics
Nucleoside Diphosphate Sugars - isolation & purification
Nucleoside Diphosphate Sugars - metabolism
Transferases (Other Substituted Phosphate Groups) - metabolism
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Summary:Two birds with one stone: Four DNA aptamers were isolated for Bcs1, a bifunctional enzyme that catalyzes both the reduction of ribulose 5‐phosphate by using NADPH and cytidylyltransfer by using CTP. The inhibitory effects of these aptamers towards Bcs1 and their secondary structural properties were investigated (see scheme).
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200700257