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Literature summary for 6.3.5.4 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

Inhibitors Comment Organism Structure
AMP product inhibition Rattus norvegicus
Asn product inhibition Rattus norvegicus
Glu product inhibition Rattus norvegicus

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

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