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Literature summary extracted from

  • Ebner, E.; Wolf, D.; Gancedo, C.; Elsässer, S.; Holzer, H.
    ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties (1970), Eur. J. Biochem., 14, 535-544.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.42 L-glutamine highly activating Escherichia coli
2.7.7.42 L-glutamine activator of adenylylation Escherichia coli

General Stability

EC Number General Stability Organism
2.7.7.42 bovine serum albumin, above 1 mg/ml, prevents inactivation at 4°C and 25°C and aggregation Escherichia coli
2.7.7.42 Mg2+, 20 mM protects to some extent against heat inactivation Escherichia coli
2.7.7.42 no stabilization by ATP, CTP, Mn2+, glutamine, cysteine or mercaptoethanol each at 20 mM, 2 mM DTT, 20% glycerol, sucrose, polyethyleneglycol or urea at 1 M Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.42 4-Methyl-L-glutamate
-
 Escherichia coli
2.7.7.42 6-diazo-5-oxonorleucine
-
 Escherichia coli
2.7.7.42 ADP
-
 Escherichia coli
2.7.7.42 ATP inhibitory above 1 mM in presence of glutamine, not related to Mg2+ concentration Escherichia coli
2.7.7.42 CTP
-
 Escherichia coli
2.7.7.42 D-glutamine
-
 Escherichia coli
2.7.7.42 diphosphate
-
 Escherichia coli
2.7.7.42 DL-2-aminobutyric acid
-
 Escherichia coli
2.7.7.42 glutamate L- and D-isomer Escherichia coli
2.7.7.42 ITP
-
 Escherichia coli
2.7.7.42 L-methionine
-
 Escherichia coli
2.7.7.42 L-tryptophan
-
 Escherichia coli
2.7.7.42 phosphate
-
 Escherichia coli
2.7.7.42 S-(2-Hydroxyethyl)-L-cysteine
-
 Escherichia coli
2.7.7.42 sulfate
-
 Escherichia coli
2.7.7.42 UTP
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.42 0.005
-
 [L-glutamate:ammonia ligase (ADP-forming)] pH 7.6, 30°C Escherichia coli
2.7.7.42 0.15
-
 ATP pH 7.6, 30°C, in presence of glutamine Escherichia coli
2.7.7.42 0.95
-
 ATP pH 7.6, 30°C, in absence of glutamine Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.42 Mg2+ Mg2+ or Mn2+ required Escherichia coli
2.7.7.42 Mg2+ half-maximal activity at: 14 mM Escherichia coli
2.7.7.42 Mn2+ Mn2+ or Mg2+ required Escherichia coli
2.7.7.42 Mn2+ half-maximal activity at 1.4 mM Escherichia coli
2.7.7.42 additional information Ca2+, Zn2+ and Cu2+ at 10 mM are ineffective Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.42 145000
-
 gel filtration Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.42 ATP + [L-glutamate:ammonia ligase (ADP-forming)] Escherichia coli
-
 diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
 r
2.7.7.42 ATP + [L-glutamate:ammonia ligase (ADP-forming)] Escherichia coli B / ATCC 11303
-
 diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.42 Escherichia coli
-
 B
-
2.7.7.42 Escherichia coli B / ATCC 11303
-
 B
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.42 300fold to homogeneity Escherichia coli

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.42 ATP + [L-glutamate:ammonia ligase (ADP-forming)] ADP, AMP, cAMP, UTP, CTP, ITP, NAD+ cannot replace ATP Escherichia coli diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
 r
2.7.7.42 ATP + [L-glutamate:ammonia ligase (ADP-forming)] ADP, AMP, cAMP, UTP, CTP, ITP, NAD+ cannot replace ATP Escherichia coli B / ATCC 11303 diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
 r
2.7.7.42 ATP + [L-glutamate:ammonia ligase (ADP-forming)]
-
 Escherichia coli diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
 r
2.7.7.42 ATP + [L-glutamate:ammonia ligase (ADP-forming)]
-
 Escherichia coli B / ATCC 11303 diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
 r

Temperature Optimum [°C]

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

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.7.7.42 5 32
-
 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.42 7.6
-
-
 Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.7.42 5.5 9.8 pH 5.5: about 50% of activity maximum, pH 9.8: about 35% of activity maximum Escherichia coli

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.7.7.42 3
-
 4°C, 12 h, loss of 70% of initial activity Escherichia coli
2.7.7.42 4 9 4°C, 12 h, no loss of activity Escherichia coli
2.7.7.42 9.5
-
 4°C, 12 h, loss of 50% of initial activity Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.7.42 ATP absolutely required Escherichia coli
2.7.7.42 ATP inhibitory at higher comcentrations Escherichia coli