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Short Communications
Modification of E. coli phenylalanyl-tRNA synthetase by l,N6-ethenoadenosine-5'-triphosphate
1Podust V. N., 1Nevinsky G. A., 1Lavrik O. I.
  1. Institute of Bioorganic Chemistry, Siberian Branch of the Academy of Sciences of the USSR
    Novosibirsk, USSR


The irradiation of phenylalanyl-tRNA synthetase by nitrogen laser light (X337 nm) in the presence of e ATP results in enzyme inactivation and covalent attachement of nucleotide to the protein. Dependence of the enzyme photoinactivation rate on the eATP concentration is of saturated character. ATP partially protects the enzyme against covalent attachement of eATP. However none of the specific ligands (ATP, Phe, phenylalanyladenylate) prevents the enzyme inactivation.


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