EC Number   |
General Information |
Reference |
|---|
   2.7.7.42 | physiological function |
enzyme gene glnE deletion leads to a loss of activity regulation of glutamine synthetase. Additionally, the glnE mutation causes a nitrogen limitation response on the transcript level as well. Induction of the nitrogen starvation response in the mutant strain is unusually weak and signal transduction protein GlnK is present in adenylylated form even without nitrogen starvation |
722846 |
| 2.7.7.42 | physiological function |
in the presence of L-methionine sulfoximine, an inhibitor, and glutamine supplementation, a null mutant is able to grow similarly to the wild type. The GlnE mutant is able to survive and grow for extended periods in liquid medium, but not on solid medium, in the absence of glutamine synthetase inhibition |
-, 734070 |
| 2.7.7.42 | physiological function |
the adenylyltransferase and its substrate glutamine synthetase are part of a signal transduction system that includes two additional proteins, uridylyltransferase/uridylyl-removing enzyme and the PII protein |
702300 |
| 2.7.7.42 | physiological function |
the adenylyltransferase is part of the cascade that regulates the activity of glutamine synthetase, a key compound of the cells machinery for the uptake of ammonia |
705180 |
| 2.7.7.42 | physiological function |
the glutamine synthetase I activity of the glnE mutant is not down-regulated after an ammonium shock. However, the glutamine synthetase I activity of wild-type cells decreases to 60% of the original activity. GlnE mutants are glutamine prototrophic. The mutant has lost the ability for covalent glutamine synthetase I modification by adenylylation and shows an imbalance in the glutamine:glutamate ratio |
-, 734638 |
