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Literature summary for 2.7.7.42 extracted from
- Structure of the adenylylation domain of E. coli glutamine synthetase adenylyl transferase: Evidence for gene duplication and evolution of a new active site (2010), J. Mol. Biol., 396, 773-784.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| signal transduction protein PII | - |
Escherichia coli |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structure of the N-terminal domain, residues 1-440, containing the regulatory and the adenylyl transferase domains, to 2.4 A resolution. Deduction of a model of the complete enzyme and a model for the complex with glutamine synthetase and the nitrogen signal transduction protein PII | Escherichia coli |
| the structure of the C-terminal fragment, containing residues 449-946, of glutamine synthetase adenylyl transferase is determined to a resolution of 2.4 A | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + glutamine synthetase | Escherichia coli | the enzyme has two activities, adenylyl removase and adenylyl transferase, which are located in distinct catalytic domains that are separated by a regulatory domain | glutamine synthetase-AMP + diphosphate | - |
? | |
| glutamine synthetase-AMP + phosphate | Escherichia coli | the enzyme has two activities, adenylyl removase and adenylyl transferase, which are located in distinct catalytic domains that are separated by a regulatory domain | ADP + glutamine synthetase | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P30870 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | Escherichia coli | glutamine synthetase-AMP + diphosphate | - |
? | |
| 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 | Escherichia coli | ADP + glutamine synthetase | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATASE | - |
Escherichia coli |
| ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyl transferase | - |
Escherichia coli |
| GlnE | - |
Escherichia coli |
| glutamine synthetase adenylyl transferase | - |
Escherichia coli |
| glutamine synthetase ATase | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Escherichia coli |
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Release 2023.1 (January 2023)
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