Modification of E. coli phenylalanyl-tRNA synthetase by l,N6-ethenoadenosine-5'-triphosphate

Authors

  • V. N. Podust Institute of Bioorganic Chemistry, Siberian Branch of the Academy of Sciences of the USSR Novosibirsk, USSR Author
  • G. A. Nevinsky Institute of Bioorganic Chemistry, Siberian Branch of the Academy of Sciences of the USSR Novosibirsk, USSR Author
  • O. I. Lavrik Institute of Bioorganic Chemistry, Siberian Branch of the Academy of Sciences of the USSR Novosibirsk, USSR Author

DOI:

https://doi.org/10.7124/bc.00018E

Abstract

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.

References

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Published

1985-09-20

Issue

Section

Short Communications