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• W2009580930 abstract "The enzyme ATP:GTP 3′-diphosphotransferase catalyzes the transfer of the β,γ-pyrophosphate of ATP to the 3′ position of GTP or GDP. The amounts of enzyme were measured in cell extracts of a relA+ strain of E. coli grown at different growth rates between 0.4 and 1.9 generations per hour, using precipitation with specific antibodies to purify the enzyme. The amount of enzyme was found to be a constant fraction of total protein at all growth rates corresponding to about 45 molecules of enzyme per genome equivalent of DNA. The purified enzyme has little catalytic activity by itself but has to be activated either by a complex of 70S ribosomes, mRNA and uncharged tRNA or by a solvent like ethanol at a concentration of about 20%. The kinetic constants of the enzyme for the transfer pyrophosphate from ATP to GTP in the ribosome-activated state were determined. The Vmax was estimated to be 140 mol/min·mg at 37°C and the S0.5 values for GTP and ATP were 0.35 and 0.53 mM, respectively. The reaction was estimated to have an equilibrium constant of about 300. In the pyrophosphate transfer from ATP to GDP the Vmax was estimated to be 90 mol/min·mg at 37°C and the S0.5 for GDP as 0.3 mM. During amino acid starvation of a relA+ strain of E. coli the amounts of enzyme and the catalytic capacity of the enzyme are sufficient to maintain the observed ppGpp levels in the cells at all growth rates. L'enzyme ATP:GTP 3′-diphosphotransferase (le facteur stringent) catalyse le transfer du β,γ-pyrophosphate de l'ATP à la position 3′ du GTP ou du GDP. Les taux d'enzyme furent mesurés dans des extraits bruts des cellules d'E. coli, relA+ poussé à des taux de croissance entre 0,4 et 1,9 générations par heure. L'enzyme fut purifiée par précipitation avec des anticorps spécifiques. Le taux d'enzyme fut trouvé constant à tous les taux de croissance, étant 45 molécules d'enzyme par équivalent génomique d'ADN. En état purifié le facteur stringent possède en soi une activité enzymatique négligeable. Pourtant l'enzyme peut être activé soit en formant un complexe avec des ribosomes 70S, du mRNA et du tRNA non amino-acylé, soit par un solvant comme l'ethanol à 20% environ. Les constants catalytiques pour l'enzyme en complexe avec des ribosomes furent déterminés. Pour le transfert de pyrophosphate de l'ATP au GTP le Vmax est environ 140 mol/min·mg à 37°C et la valeur de S0.5 du GTP est 0,35 mM et celle d'ATP est 0,53 mM. Le constant d'équilibre fut déterminé à une valeur d'environ 300. Pour le transfert de pyrophosphate de l'ATP au GDP le Vmax est environ 90 mol/min·mg à 37°C et le S0.5 du GDP est 0,3 mM. Dans la souche d'E. coli, relA+, le taux d'enzyme et l'activité catalytique de l'enzyme sont suffisants pour créer et maintenir les niveaux de ppGpp observés pendant une carence en acides aminés dans les bactéries à tous les taux de croissances." @default.
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• W2009580930 date "1986-05-01" @default.
• W2009580930 modified "2023-09-26" @default.
• W2009580930 title "The physiology of stringent factor (ATP: GTP 3′-diphosphotransferase) in Escherichia coli" @default.
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• W2009580930 doi "https://doi.org/10.1016/s0300-9084(86)80165-1" @default.
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