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Structure and Function of Biopolymers
Interaction of fluorescent ATP and tRNA analogs with phenylalanyl-tRNA synthetase
- Institute of Bioorganic Chemistry, Siberian Branch of the Academy of Sciences of the USSR
Affinity modification of E. coli MRE-600 phenylalanyl-tRNA synthetase by 1,N6-etheno-adenosine-5-triphosphate (εATP) in the presence of different ligands has been investigated. ATP conversion into εATP results in the disturbance of specific contacts of nucle-otide with the ATP binding site in the enzyme. The εATP covalent attachment site is assumed To be situated in the tRNA 3'-terminus recognizing site. Fluorescent tRNAPhe analogs have been prepared by replacing adenosine 73 or 76 by 1,N6-ethenoadenosine. The activity of these analogs has been investigated in the aminoacylation. The low yield of photoinduced covalent attachment of these derivatives to phenylalanyl-tRNA synthetase is observed.
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