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Literature summary extracted from

  • Hongo, S.; Sato, T.
    Kinetic studies of asparagine synthetase from rat liver: role of Mg2+ in enzyme catalysis (1985), Arch. Biochem. Biophys., 238, 410-417.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.4 AMP product inhibition Rattus norvegicus
6.3.5.4 Asn product inhibition Rattus norvegicus
6.3.5.4 Glu product inhibition Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.5.4 additional information
-
 additional information
-
 Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.5.4 Mg2+ forms a complex with ATP and modifies the reaction mechanism Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.4 Rattus norvegicus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.5.4 ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate uni-uni-bi-ter ping-pong mechanism without abortive complexes. Gln binds first, followed by Glu release, and Asp and ATP bind in order followed by ordered release of diphosphate, AMP and Asn. In the presence of 0.5-2.0 mM excess Mg2+ over ATP the binding of substrates after the release of Glu is in a rapid equilibrium system Rattus norvegicus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.5.4 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.4 ATP + L-Asp + L-Gln
-
 Rattus norvegicus AMP + diphosphate + Asn + Glu
-
 ?