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Influence of the aminoacyl‐tRNA synthetase inhibitors and the diadenosine‐5'‐tetraphosphate phosphonate analogues on the catalysis of diadenosyl oligophosphates formation
Author(s) -
Biryukov A.I.,
Zhukov Yu.N.,
Lavrik O.I.,
Khomutov R.M.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81086-4
Subject(s) - biosynthesis , pyrophosphatases , adenylate kinase , chemistry , aminoacyl trna synthetase , inorganic pyrophosphatase , biochemistry , stereochemistry , enzyme , phosphonate , amino acid , transfer rna , pyrophosphate , rna , gene
Well‐known aminoacyl‐tRNA synthetase (ARSase) inhibitors, namely the analogues of amino acids and aminoacyl adenylates (aminoalkyl‐ and aminophosphonyl adenylates with K i ⋍ 0.1 μM) as well as the diadenosine 5',5'''‐ p 1 , p 4 ‐tetraphosphate (Ap 4 A) phosphonoanalogues, were for the first time used for the Ap 4 A biosynthesis regulation. Effects of a set of such compounds on lysyl‐, phenylalanyl‐ and alanyl‐tRNA synthetases from E. coli , capable of synthesizing Ap 4 A in the presence of Zn 2+ ions and pyrophosphatase, have been studied. The adenylate analogues were found to inhibit the Ap 4 A and Ap 3 A formation ( I 50 ⋍ 6 mM). Aminophosphonic and aminophosphonous acids are not involved in Ap 3 A and Ap 4 A biosynthesis and inhibited it at high concentrations. The Ap 4 A phosphoanalogues slightly inhibited the major reactions of ARSases, as well as the biosynthesis of Ap 3 A and Ap 4 A, at a concentration of 5 mM.