EC Number   |
Natural Substrates |
|---|
   2.7.7.42 | ADP + glutamine synthetase |
- |
| 2.7.7.42 | ATP + glutamine synthetase |
- |
| 2.7.7.42 | ATP + glutamine synthetase |
the enzyme has two activities, adenylyl removase and adenylyl transferase, which are located in distinct catalytic domains that are separated by a regulatory domain |
| 2.7.7.42 | ATP + [glutamine synthetase]-L-tyrosine |
- |
| 2.7.7.42 | ATP + [L-glutamate:ammonia ligase (ADP-forming)] |
- |
| 2.7.7.42 | ATP + [L-glutamate:ammonia ligase (ADP-forming)] |
enzyme is involved in the regulation of nitrogen assimilation |
| 2.7.7.42 | ATP + [L-glutamate:ammonia ligase (ADP-forming)] |
inactivation of [L-glutamate:ammonia ligase (ADP-forming)] by attachment of the adenylyl moiety of ATP |
| 2.7.7.42 | ATP + [L-glutamate:ammonia ligase (ADP-forming)] |
enzyme is responsible for regulation of [L-glutamate:ammonia ligase (ADP-forming)] activity |
| 2.7.7.42 | glutamine synthase + ATP |
ATase primarily regulated by alpha-ketoglutarate, glutamine has no effect on neither the adenylylation nor the deadenylylation of glutamine synthetase, PII proteins only stimulate the adenylylation reaction |
| 2.7.7.42 | glutamine synthetase-AMP + phosphate |
the enzyme has two activities, adenylyl removase and adenylyl transferase, which are located in distinct catalytic domains that are separated by a regulatory domain |
