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Effects of uridylyltransferase and adenylyltransferase on the synthesis of glutamine synthetase in escherichia coli


, : Effects of uridylyltransferase and adenylyltransferase on the synthesis of glutamine synthetase in escherichia coli. Federation Proceedings 44(3): 682



Accession: 028228351

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Related references

Rhee, S.G.; Park, S.C.; Koo, J.H., 1985: The role of adenylyltransferase and uridylyltransferase in the regulation of glutamine synthetase in Escherichia coli. The regulation of GS activity involves two nucleotidylation cycles, the uridylylation cycle of PII and the adenylylation cycle of GS, which are catalyzed by two converter enzymes, uridylyltransferase and adenylyltransferase, respectively. The conv...

Magasanik, B.; Bueno, R., 1985: The role of uridylyltransferase and PII in the regulation of the synthesis of glutamine synthetase in Escherichia coli. Current Topics in Cellular Regulation 27: 215-220

Wolf, D.; Ebner, E., 1972: Effect of effectors and substrate regulating the inactivation of glutamine synthetase from Escherichia coli: conformation changes of ATP:glutamine synthetase-adenylyltransferase. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 353(5): 770-771

Jiang, P.; Mayo, A.E.; Ninfa, A.J., 2007: Escherichia coli Glutamine Synthetase Adenylyltransferase (ATase, EC 2.7.7.49): Kinetic Characterization of Regulation by PII, PII-UMP, Glutamine, and a-Ketoglutarate. Biochemistry (American Chemical Society) 46(13): 33-46

Jiang, P.; Mayo, A.E.; Ninfa, A.J., 2007: Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and alpha-ketoglutarate. Glutamine synthetase adenylyltranferase (ATase, EC 2.7.7.49) catalyzes the adenylylation and deadenylylation of glutamine synthetase (GS), regulating GS activity. The adenylyltransferase (AT) reaction is activated by glutamine and by the unmodifi...

Ebner, E.; Wolf, D.; Gancedo, C.; Elsässer, S.; Holzer, H., 1970: ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties. European Journal of Biochemistry 14(3): 535-544

Xu, Y.; Zhang, R.; Joachimiak, A.; Carr, P.D.; Huber, T.; Vasudevan, S.G.; Ollis, D.L., 2004: Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase. We report the crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase that catalyzes the reversible nucleotidylation of glutamine synthetase (GS), a key enzyme in nitrogen assimilation. This domain (AT-N440) catalyzes th...

Wolf, D.; Ebner, E.; Hinze, H., 1972: Inactivation, stabilization and some properties of ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. European Journal of Biochemistry 25(2): 239-244

Bloom, F.R.; Levin, M.S.; Foor, F.; Tyler, B., 1978: Regulation of glutamine synthetase formation in Escherichia coli: characterization of mutants lacking the uridylyltransferase. A lambda phage (lambdaNK55) carrying the translocatable element Tn10, conferring tetracycline resistance (Tetr), has been utilized to isolate glutamine auxotrophs of Escherichia coli K-12. Such strains lack uridylyltransferase as a result of an in...

Caban, C.E.; Ginsburg, A., 1976: Glutamine synthetase adenylyltransferase from Escherichia coli: purification and physical and chemical properties. The glutamine synthetase adenylyltransferase (EC 2.7.7.42), WHIch catalyzes the adenylylation and deadenylylation of glutamine synthetase in E. coli, has been stabilized and purified 2200-fold to apparent homogeneity. Sedimentation and electrophor...