Biopolymers and cell. 1988. Volume 4. № 4. 197 - 203

V. N. Ankilova, V. A. Gordienko, 0. I. Lavrik, N. A. Moor

INTERACTION OF FLUORESCENT ATP AND tRNA ANALOGS WITH PHENYLALANYL-tRNA SYNTHETASE

Summary

    Affinity modification of E. coli MRE-600 phenylalanyl-tRNA synthetase by l,N6-etheno-adenosine-5-triphosphate (sATP) in the presence of different ligands has been investigated. ATP conversion into eATP results in the disturbance of specific contacts of nucle-otide with the ATP binding site in the enzyme. The eATP 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 l,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.