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- W2058634501 abstract "Effector-activated ribozymes that respond to small organic molecules have previously been generated by appending binding species (aptamers) to ribozymes. In order to determine if deoxyribozymes can similarly be activated by effector molecules, we have appended an anti-adenosine aptamer to a selected deoxyribozyme ligase. The resultant constructs are specifically activated by ATP. Optimization of the joining region resulted in ligases that are activated up to 460-fold by ATP. The selected deoxyribozyme catalyzes ligation largely via a templating mechanism. Effector activation is surprisingly achieved by suppression of the rate of the background, templated ligation reaction in the absence of the effector molecule, probably by misalignment of the oligonucleotide substrates. This novel allosteric mechanism has not previously been observed for nucleic-acid catalysts and is rare even in protein catalysts." @default.
- W2058634501 created "2016-06-24" @default.
- W2058634501 creator A5039254274 @default.
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- W2058634501 date "2002-04-01" @default.
- W2058634501 modified "2023-10-16" @default.
- W2058634501 title "ATP-Dependent Allosteric DNA Enzymes" @default.
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- W2058634501 doi "https://doi.org/10.1016/s1074-5521(02)00123-0" @default.
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