Biopolym. Cell. 1985; 1(5):267-270.
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

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

[1] Ivanov M. V. Kost AA Investigation proteins by etenoproizvodnyh adenine and ditozina. Usp Sovrem Biol., 1980, 21:112-129.
[2] Nevinsky G A., Podust V. N., Ankilova V. N., Lavrik O. I. Phenylalanyl-tRNA synthetase from E. coli: enzyme modification by chemically reactive analogs of fluorescent nucleotides. Russian Journal of Bioorganic Chemistry. 1983; 9(7):936-946.
[3] Nevinskii GA, Podust VN, Khodyreva SN, Gorshkova II, Lavrik OI. Adenosine- and ethenoadenosine-5'-trimetaphosphates: the effect of covalent bond formation on the state of the affinity label in the complex with phenylalanyl-tRNA-synthetase. Mol Biol (Mosk). 1984;18(5):1311-5.
[4] Ankilova VN, Lavrik OI, Khodyreva SN. Purification and properties of phenylalanyl-tRNA-synthetase from Escherichia coli MRE-600. Prikl Biokhim Mikrobiol. 1984;20(2):208-16.
[5] Sandakhchiev LS, Starostin VK, Stefanovic LE, Chuchaev BM. Application sorption on aminoethyl cellulose to isolate mRNA from the aqueous layer after phenol extraction. Mol Biol (Mosk), 1967; 1(4):463-466.
[6] Khodyreva SN, Nevinskii GA, Ankilova VN, Lavrik OI. Modification of phenylalanyl-tRNA-synthetase from Escherichia coli MRE600 by adenosine-5'-trimetaphosphate. Mol Biol (Mosk). 1983;17(6):1196-203.
[7] Vlasov VV, Grachev MA, Lavrik OI et al. Affinity modification of biopolymers. Nauka, Novosibirsk, 1983. 244.
[8] Kitz R, Wilson IB. Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase. J Biol Chem. 1962;237:3245-9.