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Literature summary for 2.7.7.42 extracted from

  • Caban, C.E.; Ginsburg, A.
    Glutamine synthetase adenylyltransferase from Escherichia coli: purification and physical and chemical properties (1976), Biochemistry, 15, 1569-1580.
    View publication on PubMed

Activating Compound

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

General Stability Organism
considerably less stable in Tris or imidazole buffer than in a magnesium phosphate buffer Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate inhibition of adenylylation, activation of deadenylylation Escherichia coli

Metals/Ions

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
2200fold to homogeneity Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli

Storage Stability

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 and Products (Substrate)

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

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.2 adenylylation Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP activator of adenylylation Escherichia coli

pI Value

Organism Comment pI Value Maximum pI Value
Escherichia coli
-
-
4.98