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Literature summary for 6.3.4.16 extracted from

  • Britton, H.G.; Rubio, V.
    Carbamoyl-phosphate synthetase I. Kinetic of binding and dissociation of acetylglutamate and of activation and deactivation (1988), Eur. J. Biochem., 171, 615-622.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
acetylglutamate little activity at physiological concentrations of substrates in absence of acetylglutamate Rattus norvegicus
acetylglutamate acetylglutamate does not dissociate with each turnover of the enzyme Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Cs+ monovalent cation required, ATP hydrolysis is activated in the order of the series: Tl+, Cs+, Rb+, K+, Na+. Half-maximal activation at 1-2 mM Rattus norvegicus
K+ monovalent cation required, ATP hydrolysis is activated in the order of the series: Tl+, Cs+, Rb+, K+, Na+. Half-maximal activation at 1-2 mM Rattus norvegicus
Na+ monovalent cation required, ATP hydrolysis is activated in the order of the series: Tl+, Cs+, Rb+, K+, Na+ Rattus norvegicus
Rb+ monovalent cation required, ATP hydrolysis is activated in the order of the series: Tl+, Cs+, Rb+, K+, Na+. Half-maximal activation at 1-2 mM Rattus norvegicus
Tl+ monovalent cation required, ATP hydrolysis is activated in the order of the series: Tl+, Cs+, Rb+, K+, Na+. Half-maximal activation at 0.2-0.6 mM Rattus norvegicus

Organism

Organism UniProt Comment Textmining
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 + NH4+ + CO2 + H2O
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Rattus norvegicus ADP + phosphate + carbamoylphosphate
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