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Literature summary for 2.7.7.42 extracted from

  • Wolf, D.H.; Ebner, E.
    Studies on the reaction mechanism of adenosine triphosphate: glutamine synthetase adenylyltransferase from Escherichia coli B. Conformational changes elicited by effectors and substrates: reactivity of sulfhydryl groups (1972), J. Biol. Chem., 247, 4208-4212.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
L-glutamine establishes feed-back control by stimulating the adenylylation and inactivation of the [L-glutamate:ammonia ligase (ADP-forming)] Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-oxoglutarate slight activation at 20 mM Escherichia coli
3-phosphoglycerate 66% inhibition at 20 mM Escherichia coli
ATP 74% inhibition at 20 mM Escherichia coli
diphosphate 28% inhibition at 2 mM Escherichia coli
UTP 48% inhibition at 10 mM Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ stimulates 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 inactivation of [L-glutamate:ammonia ligase (ADP-forming)] by attachment of the adenylyl moiety of ATP diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
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r

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
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Escherichia coli diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
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r
ATP + [L-glutamate:ammonia ligase (ADP-forming)] inactivation of [L-glutamate:ammonia ligase (ADP-forming)] by attachment of the adenylyl moiety of ATP Escherichia coli diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
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r

Cofactor

Cofactor Comment Organism Structure
ATP inhibitory at higher comcentrations Escherichia coli