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Literature summary extracted from

  • Jiang, P.; Mayo, A.E.; Ninfa, A.J.
    Escherichia coli glutamine synthetase adenylyltransferase (ATase, EC 2.7.7.49): kinetic characterization of regulation by PII, PII-UMP, glutamine, and alpha-ketoglutarate (2007), Biochemistry, 46, 4133-4146.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.42 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
2.7.7.42 alpha-ketoglutarate 1 mM Escherichia coli
2.7.7.42 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
2.7.7.42 glutamine activates the adenylyltransferase reaction Escherichia coli
2.7.7.42 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
2.7.7.42 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
2.7.7.42 PII signal transduction protein 0.0004 mM, activates the adenylyltransferase reaction Escherichia coli
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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
2.7.7.89 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
2.7.7.89 uridylated signal transduction protein PII the adenylyl-removing reaction is activated by PII-UMP and is inhibited by glutamine and by 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.42 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
2.7.7.42 glutamine inactivates the adenylyl-removing reaction Escherichia coli
2.7.7.42 signal transduction protein PII inactivates the adenylyl-removing reaction Escherichia coli
2.7.7.42 signal transduction protein PII-UMP reaction is inhibited by signal transduction protein PII-UMP Escherichia coli
2.7.7.42 uridylated PII signal transduction protein inhibits the adenylyltransferase reaction Escherichia coli
2.7.7.42 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
2.7.7.89 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
2.7.7.89 glutamine the adenylyl-removing reaction is activated by PII-UMP and is inhibited by glutamine and by PII. 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
2.7.7.89 signal transduction protein PII the adenylyl-removing reaction is activated by PII-UMP and is inhibited by glutamine and by 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.42 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
2.7.7.42 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
2.7.7.42 0.0032
-
 glutamine synthetase pH 7.5, 30°C Escherichia coli
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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
2.7.7.42 1.1
-
 ATP pH 7.5, 30°C Escherichia coli
2.7.7.42 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
2.7.7.89 0.009
-
 [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine pH 7.5, 30°C Escherichia coli
2.7.7.89 0.33
-
 phosphate pH 7.5, 30°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.42 K+ adenylyltransferase and adenylyl-removing assay with 10 mM KCl Escherichia coli
2.7.7.42 Mg2+ adenylyltransferase and adenylyl-removing assay with 10 mM MgCl2 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.42 Escherichia coli
-
-
-
2.7.7.89 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.42 adenylyl-[glutamine synthase] + phosphate deadenylylation reaction Escherichia coli glutamine synthase + ADP
-
 r
2.7.7.42 ATP + glutamine synthetase
-
 Escherichia coli adenylated glutamine synthetase + diphosphate
-
 ?
2.7.7.42 ATP + [L-glutamate:ammonia ligase (ADP-forming)]
-
 Escherichia coli diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
 ?
2.7.7.42 glutamine synthase + ATP adenylylation reaction Escherichia coli adenylyl-[glutamine synthase] + diphosphate
-
 r
2.7.7.89 [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine + phosphate
-
 Escherichia coli [L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine + ADP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.42 adenylyltransferase
-
 Escherichia coli
2.7.7.42 ATASE
-
 Escherichia coli
2.7.7.42 glutamine synthetase adenylyltransferase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.42 30
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.42 7.5
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.7.42 ATP
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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
2.7.7.42 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