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Ishige, K., Noguchi, T. (2000) Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli. Proceedings of the National Academy of Sciences, 97 (26) 14168-14171 doi:10.1073/pnas.011518098

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Reference TypeJournal (article/letter/editorial)
TitleInorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli
JournalProceedings of the National Academy of Sciences
AuthorsIshige, K.Author
Noguchi, T.Author
Year2000 (December 19)Volume97
Issue26
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.011518098Search in ResearchGate
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Mindat Ref. ID1649968Long-form Identifiermindat:1:5:1649968:9
GUID0
Full ReferenceIshige, K., Noguchi, T. (2000) Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli. Proceedings of the National Academy of Sciences, 97 (26) 14168-14171 doi:10.1073/pnas.011518098
Plain TextIshige, K., Noguchi, T. (2000) Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli. Proceedings of the National Academy of Sciences, 97 (26) 14168-14171 doi:10.1073/pnas.011518098
In(2000, December) Proceedings of the National Academy of Sciences Vol. 97 (26) Proceedings of the National Academy of Sciences

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Ishige, K., Zhang, H., Kornberg, A. (2002) Polyphosphate kinase (PPK2), a potent, polyphosphate-driven generator of GTP. Proceedings of the National Academy of Sciences, 99 (26) 16684-16688 doi:10.1073/pnas.262655299
Zhang, H., Ishige, K., Kornberg, A. (2002) A polyphosphate kinase (PPK2) widely conserved in bacteria. Proceedings of the National Academy of Sciences, 99 (26) 16678-16683 doi:10.1073/pnas.262655199
Kuroda, A., Kornberg, A. (1997) Polyphosphate kinase as a nucleoside diphosphate kinase in Escherichia coli and Pseudomonas aeruginosa. Proceedings of the National Academy of Sciences, 94 (2) 439-442 doi:10.1073/pnas.94.2.439
Kumble, K. D., Ahn, K., Kornberg, A. (1996) Phosphohistidyl active sites in polyphosphate kinase of Escherichia coli. Proceedings of the National Academy of Sciences, 93 (25) 14391-14395 doi:10.1073/pnas.93.25.14391
Dannelly, H. K., Roseman, S. (1992) NAD+ and NADH regulate an ATP-dependent kinase that phosphorylates enzyme I of the Escherichia coli phosphotransferase system. Proceedings of the National Academy of Sciences, 89 (23) 11274-11276 doi:10.1073/pnas.89.23.11274
Greenberg, G. R., Somerville, R. L. (1962) DEOXYURIDYLATE KINASE ACTIVITY AND DEOXYURIDINETRIPHOSPHATASE IN ESCHERICHIA COLI. Proceedings of the National Academy of Sciences, 48 (2) 247-257 doi:10.1073/pnas.48.2.247
Kuroda, A., Tanaka, S., Ikeda, T., Kato, J., Takiguchi, N., Ohtake, H. (1999) Inorganic polyphosphate kinase is required to stimulate protein degradation and for adaptation to amino acid starvation in Escherichia coli. Proceedings of the National Academy of Sciences, 96 (25) 14264-14269 doi:10.1073/pnas.96.25.14264
Sproul, A. A., Lambourne, L. T. M., Jean-Jacques D, J., Kornberg, H. L. (2001) Genetic control of manno(fructo)kinase activity in Escherichia coli. Proceedings of the National Academy of Sciences, 98 (26) 15257-15259 doi:10.1073/pnas.211569798
Zhu, Y., Qin, L., Yoshida, T., Inouye, M. (2000) Phosphatase activity of histidine kinase EnvZ without kinase catalytic domain. Proceedings of the National Academy of Sciences, 97 (14) 7808-7813 doi:10.1073/pnas.97.14.7808
Kit, S., Otsuka, H., Qavi, H., Hazen, M. (1981) Herpes simplex virus thymidine kinase activity of thymidine kinase-deficient Escherichia coli K-12 mutant transformed by hybrid plasmids. Proceedings of the National Academy of Sciences, 78 (1) 582-586 doi:10.1073/pnas.78.1.582
Peterkofsky, A., Gazdar, C. (1975) Interaction of enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system with adenylate cyclase of Escherichia coli. Proceedings of the National Academy of Sciences, 72 (8) 2920-2924 doi:10.1073/pnas.72.8.2920
 
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