EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  2.7.7.89 | adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O |
- |
Escherichia coli |
adenylate + [L-glutamate:ammonia ligase (ADP-forming)] |
- |
ir |
| 2.7.7.89 | adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O |
- |
Escherichia coli |
adenylate + [L-glutamate:ammonia ligase (ADP-forming)] |
the primary product may be ADP which is then degraded to AMP |
ir |
| 2.7.7.89 | adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O |
activation of adenylated glutamine synthetase, EC 6.3.1.2, which is less active in catalyzing glutamine biosynthesis |
Escherichia coli |
? |
- |
? |
| 2.7.7.89 | more |
the bifunctional adenylyltransferase ATase, product of glnE, catalyzes the adenylylation of glutamine synthetase and the deadenylylation of glutamine synthetase-AMP. The adenylylation reaction is activated by PII signal transduction protein, while the deadenylylation reaction requires PII-UMP. Both of these reactions are stimulated by 2-oxoglutarate and ATP |
Escherichia coli |
? |
- |
? |
| 2.7.7.89 | [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine + H2O |
- |
Escherichia coli |
adenylate + [L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine |
- |
? |
| 2.7.7.89 | [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine + phosphate |
- |
Escherichia coli |
[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine + ADP |
- |
? |
