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Cleavage of an amide bond by a ribozymeA variant form of a group I ribozyme, optimized by in vitro evolution for its ability to catalyze magnesium-dependent phosphoester transfer reactions involving DNA substrates, also catalyzes the cleavage of an unactivated alkyl amide when that linkage is presented in the context of an oligodeoxynucleotide analog. Substrates containing an amide bond that joins either two DNA oligos, or a DNA oligo and a short peptide, are cleaved in a magnesium-dependent fashion to generate the expected products. The first-order rate constant, kcat, is 0.1 x 10(-5) min-1 to 1 x 10(-5) min-1 for the DNA-flanked substrates, which corresponds to a rate acceleration of more than 10(3) as compared with the uncatalyzed reaction.
Document ID
20050000243
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Dai, X.
(Scripps Research Institute La Jolla, CA 92037)
De Mesmaeker, A.
Joyce, G. F.
Miller, S. L.
Date Acquired
August 22, 2013
Publication Date
January 13, 1995
Publication Information
Publication: Science
Volume: 267
Issue: 5195
ISSN: 0036-8075
Subject Category
Exobiology
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Exobiology
Non-NASA Center

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