Activating Compound | Comment | Organism | Structure |
---|---|---|---|
L-glutamine | required | Escherichia coli | |
L-glutamine | in presence of saturating amounts of PIIA protein Mg2+-supported activity is activated, Mn2+-supported activity is almost unchanged | Escherichia coli | |
L-glutamine | activator of adenylylation | Escherichia coli | |
PII regulatory protein | 3-5fold stimulation without glutamine, pH-independent in the range of pH 7.2-8.5 | Escherichia coli |
General Stability | Organism |
---|---|
considerably less stable in Tris or imidazole buffer than in a magnesium phosphate buffer | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-oxoglutarate | inhibition of adenylylation, activation of deadenylylation | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | stimulates | Escherichia coli | |
Mg2+ | Mg2+ or Mn2+ required | Escherichia coli | |
Mn2+ | stimulates | Escherichia coli | |
Mn2+ | Mn2+ or Mg2+ required | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
64000 | - |
low and high speed sedimentation equilibrium, 115000 MW enzyme form is slowly converted during storage at 4°C to a smaller protein that is active only in adenylylation, not in deadenylylation | Escherichia coli |
114000 | - |
1 * 114000, high speed sedimentation study of the enzyme in 6 M guanidine-HCl | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [L-glutamate:ammonia ligase (ADP-forming)] | Escherichia coli | - |
diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP) | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
2200fold to homogeneity | Escherichia coli |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Escherichia coli |
Storage Stability | Organism |
---|---|
-80°C, purified enzyme, stored after quick freezing with liquid N2, potassium phosphate buffer, 10-100 mM, pH 7.6, 1 mM MgCl2, stable for months at enzyme concentration above 0.1 mg/ml | Escherichia coli |
0°C-4°C, enzyme concentration above 1 mg/ml, stable for 12 days | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [L-glutamate:ammonia ligase (ADP-forming)] | - |
Escherichia coli | diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP) | - |
? | |
ATP + [L-glutamate:ammonia ligase (ADP-forming)] | - |
Escherichia coli | diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP) | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 114000, high speed sedimentation study of the enzyme in 6 M guanidine-HCl | Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | 8.2 | adenylylation | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | activator of adenylylation | Escherichia coli |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Escherichia coli | - |
- |
4.98 |