Abstract: It was shown that N chlorambucilyl [14C]phenylalanyl tRNA at pH 5.8 forms a complex with phenylalanine: tRNA ligase (EC 6.1.1) from E. coli MRE 600, and when contained in the complex is capable of highly effectively alkylating the enzyme. The alkylation of the enzyme leads to specific inactivation of phenylalanine:tRNA ligase. The inactivation of lysine: and valine: tRNA ligases is not observed. In the process of alkylation of phenylalanine:tRNA ligase there is a proportionate decrease in the catalytic activity of the enzyme in reactions of ATP [32P] pyrophosphate exchange, acylation of tRNA, and deacylation of [14C]phenylalanyl tRNA, which may be evidence of an interrelationship of the centers that carry out various catalytic functions of ligase. The inactivation of ligase Phe by CBP-tRNA under the optimum conditions of the aminoacylation of tRNA (pH 7.5) was detected. It was shown that the effectiveness of complex formation of the enzyme with CBP-tRNA decreases in the presence of tRNA.

Cite: Gorshkova I.I. , Lavrik O.I. , Nevinskii G.A. , Khutoryanskaya L.Z.
Specific modification of phenylalanine:tRNA ligase from E. coli MRE 600 with N chlorambucilyl [14C]phenylalanyl tRNA
Molecular Biology. 1975. V.9. N4. P.409-414. Scopus

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Scopus:

2-s2.0-0016787439

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