Diadenosine oligophosphates: peculiarities of synthesis by phenylalanyl-tRNA synthetases from E. coli MRE-600 and Thermus thermophilus HB8.
Temperature and other factors affecting synthesis of bis(5'-adenosyl) tetraphosphate (Ap4A) and bis(5'-adenosyl)triphosphate (Ap3A) catalyzed by phenylalanyl-tRNA synthetases (PheRSs) from Escherichia coli MRE-600 and Thermus thermophilus HB8 have been investigated. Those two synthetases exhibited different temperature-dependent rates of the Ap4A and Ap3A synthesis. However, with respect to the effects of such effectors of the Ap4A synthesis as Zn2+, Mg2+, tRNA and Ap4A phosphonate analogues, as well as some inhibitors of aminoacyl-tRNA synthetase, those two enzymes were apparently undistinguishable.
Biryukov
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W.A. Engelhardt Institute of Molecular Biology, USSR Academy of Sciences, Moscow.
Ankilova
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Lavrik
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D015226:Dinucleoside Phosphates / Q000096:biosynthesis*; D004926:Escherichia coli / Q000201:enzymology*; D007202:Indicators and Reagents; D007700:Kinetics; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism*; D013816:Thermodynamics; D016963:Thermus thermophilus / Q000201:enzymology*
D015226:Dinucleoside Phosphates; D007202:Indicators and Reagents; C020733:diadenosine tetraphosphate; C011440:diadenosine triphosphate; D010652:Phenylalanine-tRNA Ligase