EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.89 | 2-oxoglutarate | activation | Escherichia coli | |
2.7.7.89 | adenosine | activation by nucleotides, most efficient in presence of two different nucleotides | Escherichia coli | |
2.7.7.89 | GTP | activation by nucleotides, most efficient in presence of two different nucleotides | Escherichia coli | |
2.7.7.89 | ITP | activation by nucleotides, most efficient in presence of two different nucleotides | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.89 | diphosphate | - |
Escherichia coli | |
2.7.7.89 | glutamate | - |
Escherichia coli | |
2.7.7.89 | glutamine | - |
Escherichia coli | |
2.7.7.89 | SO42- | - |
Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.7.89 | 0.004 | - |
Adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] | calculated as adenylyl groups removed from substrate | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.89 | arsenate | activation | Escherichia coli | |
2.7.7.89 | Mg2+ | activation | Escherichia coli | |
2.7.7.89 | Mn2+ | activation | Escherichia coli | |
2.7.7.89 | additional information | not activated by Ca2+, Cd2+, Zn2+, Ba2+ | Escherichia coli | |
2.7.7.89 | phosphate | activation | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.89 | adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O | Escherichia coli | activation of adenylated glutamine synthetase, EC 6.3.1.2, which is less active in catalyzing glutamine biosynthesis | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.89 | Escherichia coli | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.7.89 | - |
Escherichia coli |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.7.7.89 | 0.015 | - |
- |
Escherichia coli |
EC Number | Storage Stability | Organism |
---|---|---|
2.7.7.89 | 4°C, 2 weeks | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 | ? | - |
? |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.7.89 | 7.3 | - |
- |
Escherichia coli |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
2.7.7.89 | 6.5 | 8 | 80% of maximal activity at pH 6.5, 50% of maximal activity at pH 8.0 | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.89 | ADP | activation by nucleotides, most efficient in presence of two different nucleotides | Escherichia coli | |
2.7.7.89 | AMP | activation by nucleotides, most efficient in presence of two different nucleotides | Escherichia coli | |
2.7.7.89 | ATP | activation by nucleotides, most efficient in presence of two different nucleotides | Escherichia coli | |
2.7.7.89 | CTP | activation by nucleotides, most efficient in presence of two different nucleotides | Escherichia coli | |
2.7.7.89 | UTP | activation by nucleotides, most efficient in presence of two different nucleotides | Escherichia coli |