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Hydrolysis of tRNA(sup Phe) on Suspensions of Amino AcidsRNA is adsorbed strongly on suspensions of many moderately soluble organic solids. In some cases, the hydrolysis of tRNA(sup Phe) is greatly accelerated by adsorption, and the major sites of hydrolysis are changed from those that are important in homogeneous solution. Here we show that the hydrolysis is greatly accelerated by suspensions of aspartic acid and beta-glutamic acid but not by suspensions of alpha-glutamic acid, asparagine, or glutamine. The non-enzymatic hydrolysis of RNA has been studied extensively, especially because of its relevance to the mechanisms of action of ribozymes and to biotechnology and therapy. Many ribonucleases, ribozymes, and non-biological catalysts function via acid-base catalysis of an intramolecular transesterification mechanism in which the 2'-OH group attacks the adjacent phosphate group. The pentacoordinated phosphorane intermediate may collapse back to starting material, or yield isomerized or cleaved products.
Document ID
20030067939
Acquisition Source
Headquarters
Document Type
Reprint (Version printed in journal)
Authors
Gao, Kui
(Salk Inst. for Biological Studies San Diego, CA, United States)
Orgel, Leslie E.
(Salk Inst. for Biological Studies San Diego, CA, United States)
Date Acquired
August 21, 2013
Publication Date
January 1, 2001
Publication Information
Publication: Helvetica Chimica Acta
Volume: 84
Subject Category
Life Sciences (General)
Funding Number(s)
CONTRACT_GRANT: NAGW-1660
CONTRACT_GRANT: NAG5-4546
CONTRACT_GRANT: NAGW-2881
Distribution Limits
Public
Copyright
Other

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