Activating Compound | Comment | Organism | Structure |
---|---|---|---|
2-oxoglutarate | controls the extent of activation or inhibition of the enzyme by PII or PII-UMP. 2-oxoglutarate acts exclusively through its binding to PII and PII-UMP, and does not alter the binding of PII or PII-UMP to the enzyme | Escherichia coli | |
alpha-ketoglutarate | 1 mM | Escherichia coli | |
alpha-ketoglutarate | regulates both adenylyltransferase and adenylyl-removing reaction, acts through its binding to signal transduction protein PII and signal transduction protein PII-UMP does not alter the binding of signal transduction protein PII or signal transduction protein PII-UMP to the enzyme, adenylyltransferase assay with 0.05 mM and adenylyl-removing assay with 1 mM alpha-ketoglutarate | Escherichia coli | |
glutamine | activates the adenylyltransferase reaction | Escherichia coli | |
glutamine | the adenylyltransferase reaction is activated by glutamine and by the unmodified form of the PII signal transduction protein and is inhibited by the uridylylated form of PII, PII-UMP. PII, PII-UMP, and glutamine shift the enzyme among at least six different enzyme forms, two of which are inactive, one of which exhibits adenylyl-removing activity, and three of which exhibit adenylyltranferase activity. The PII, PII-UMP, and glutamine binding sites are in communication. Glutamine and PII-UMP compete for the enzyme | Escherichia coli | |
L-glutamine | adenylyltransferase reaction is activated by glutamine, enzyme contains one site for glutamine, sites of signal transduction protein PII, signal transduction protein PII-UMP and glutamine are in communication, glutamine favours binding of signal transduction protein PII but competes with signal transduction protein PII-UMP for the enzyme | Escherichia coli | |
PII signal transduction protein | 0.0004 mM, activates the adenylyltransferase reaction | Escherichia coli | |
signal transduction protein PII | adenylyltransferase reaction is activated by signal transduction protein PII, binding of signal transduction protein PII is favoured by glutamine and reduced by signal transduction protein PII-UMP, enzyme appears to have two distinct sites for signal transduction protein PII and signal transduction protein PII-UMP | Escherichia coli | |
signal transduction protein PII | the adenylyltransferase reaction is activated by glutamine and by the unmodified form of the PII signal transduction protein and is inhibited by the uridylylated form of PII, PII-UMP. PII, PII-UMP, and glutamine shift the enzyme among at least six different enzyme forms, two of which are inactive, one of which exhibits adenylyl-removing activity, and three of which exhibit adenylyltranferase activity. The enzyme appears to contain two distinct sites for PII and PII-UMP. The PII, PII-UMP, and glutamine sites are in communication. The binding of PII is favored by glutamine and its level reduced by PII-UMP, whereas glutamine and PII-UMP compete for the enzyme | Escherichia coli | |
signal transduction protein PII-UMP | activates the adenylyl-removing reaction, enzyme appears to have two distinct sites for signal transduction protein PII and signal transduction protein PII-UMP | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-oxoglutarate | controls the extent of activation or inhibition of the enzyme by PII or PII-UMP. 2-Oxoglutarate acts exclusively through its binding to PII and PII-UMP, and does not alter the binding of PII or PII-UMP to the enzyme | Escherichia coli | |
glutamine | inactivates the adenylyl-removing reaction | Escherichia coli | |
signal transduction protein PII | inactivates the adenylyl-removing reaction | Escherichia coli | |
signal transduction protein PII-UMP | reaction is inhibited by signal transduction protein PII-UMP | Escherichia coli | |
uridylated PII signal transduction protein | inhibits the adenylyltransferase reaction | Escherichia coli | |
uridylated signal transduction protein PII | the adenylyltransferase reaction is activated by glutamine and by the unmodified form of the PII signal transduction protein and is inhibited by the uridylylated form of PII, PII-UMP. PII, PII-UMP, and glutamine shift the enzyme among at least six different enzyme forms, two of which are inactive, one of which exhibits adenylyl-removing activity, and three of which exhibit adenylyltranferase activity. The enzyme appears to contain two distinct sites for PII and PII-UMP. The PII, PII-UMP, and glutamine sites are in communication. The binding of PII is favored by glutamine and its level reduced by PII-UMP, whereas glutamine and PII-UMP compete for the enzyme | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0009 | - |
adenylyl-[glutamine synthase] | adenylyl-removing activity, 0.00002 mM ATase, 1 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII-UMP, 1 mM ATP, 5 mM potassium phosphate | Escherichia coli | |
0.0029 | - |
glutamine synthase | adenylyltransferase activity, 0.5 mM ATP, 0.05 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII, 0.00008 mM ATase | Escherichia coli | |
0.0032 | - |
glutamine synthetase | pH 7.5, 30°C | Escherichia coli | |
0.0034 | - |
glutamine synthase | adenylyltransferase activity, 0.5 mM ATP, 0.05 mM alpha-ketoglutarate, 0.005 mM signal transduction protein PII, 0.0001 mM ATase | Escherichia coli | |
0.0035 | - |
glutamine synthase | adenylyltransferase activity, 0.5 mM ATP, 0.05 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII, 0.0001 mM ATase | Escherichia coli | |
0.006 | - |
glutamine synthase | adenylyltransferase activity, 3.5 mM ATP, 0.05 mM alpha-ketoglutarate, 0.005 mM signal transduction protein PII, 0.00005 mM ATase | Escherichia coli | |
0.33 | - |
potassium phosphate | adenylyl-removing activity, 0.00005 mM ATase, 1 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII-UMP, 1 mM ATP, 0.00034 GS-AMP mM | Escherichia coli | |
0.75 | - |
ATP | adenylyltransferase activity, 0.0015 mM glutamine synthase, 0.05 mM alpha-ketoglutarate, 0.005 mM signal transduction protein PII, 0.0001 mM ATase | Escherichia coli | |
1.1 | - |
ATP | pH 7.5, 30°C | Escherichia coli | |
1.42 | - |
ATP | adenylyltransferase activity, 0.015 mM glutamine synthase, 0.05 mM alpha-ketoglutarate, 0.005 mM signal transduction protein PII, 0.0001 mM ATase | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | adenylyltransferase and adenylyl-removing assay with 10 mM KCl | Escherichia coli | |
Mg2+ | adenylyltransferase and adenylyl-removing assay with 10 mM MgCl2 | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
adenylyl-[glutamine synthase] + phosphate | deadenylylation reaction | Escherichia coli | glutamine synthase + ADP | - |
r | |
ATP + glutamine synthetase | - |
Escherichia coli | adenylated glutamine synthetase + diphosphate | - |
? | |
ATP + [L-glutamate:ammonia ligase (ADP-forming)] | - |
Escherichia coli | diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP) | - |
? | |
glutamine synthase + ATP | adenylylation reaction | Escherichia coli | adenylyl-[glutamine synthase] + diphosphate | - |
r |
Synonyms | Comment | Organism |
---|---|---|
adenylyltransferase | - |
Escherichia coli |
ATASE | - |
Escherichia coli |
glutamine synthetase adenylyltransferase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0008 | - |
signal transduction protein PII | inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII-UMP, 50 mM glutamine, 0.00005 mM ATase | Escherichia coli | |
0.0012 | - |
signal transduction protein PII | inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0004 mM signal transduction protein PII-UMP, 50 mM glutamine, 0.00015 mM ATase | Escherichia coli | |
0.004 | - |
signal transduction protein PII | inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII-UMP, 0.00005 mM ATase | Escherichia coli | |
0.008 | - |
signal transduction protein PII | inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0004 mM signal transduction protein PII-UMP, 0.00004 mM ATase | Escherichia coli | |
0.01 | - |
signal transduction protein PII | inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0001 mM signal transduction protein PII-UMP, 0.0001 mM ATase | Escherichia coli | |
0.08 | - |
signal transduction protein PII | inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.01 mM signal transduction protein PII-UMP, 0.00002 mM ATase | Escherichia coli | |
5 | - |
signal transduction protein PII | inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0004 mM signal transduction protein PII-UMP, 0.01 mM signal transduction protein PII, 0.0002 mM ATase | Escherichia coli | |
9 | - |
signal transduction protein PII | inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0005 mM signal transduction protein PII-UMP, 0.001 mM signal transduction protein PII, 0.00005 mM ATase | Escherichia coli | |
23 | - |
signal transduction protein PII | inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.0004 mM signal transduction protein PII-UMP, 0.00005 mM ATase | Escherichia coli | |
90 | - |
signal transduction protein PII | inhibition of adenylyl-removing activity by signal transduction protein PII, 1 mM alpha-ketoglutarate, 0.01 mM signal transduction protein PII-UMP, 0.0001 mM ATase | Escherichia coli |