Biopolym. Cell. 1988; 4(4):197-203.
Structure and Function of Biopolymers
Interaction of fluorescent ATP and tRNA analogs with phenylalanyl-tRNA synthetase
1Ankilova V. N., 1Gordienko V. A., 1Lavrik O. I., 1Moor N. A.
  1. Institute of Bioorganic Chemistry, Siberian Branch of the Academy of Sciences of the USSR
    Novosibirsk, 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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