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Literature summary extracted from

  • Lusty, C.J.
    Catalytically active monomer and dimer forms of rat liver carbamoyl-phosphate synthetase (1981), Biochemistry, 20, 3665-3675.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.4.16 acetylglutamate N-acetyl-L-glutamate displaces the equilibrium towards monomer formation Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.4.16 160000
-
 1 * 160000, sedimentation velocity measurement in presence of acetylglutamate alone, enzyme exists in a rapid, reversible monomer-dimer equilibrium. In presence of all substrates the enzyme exists as a monomer. The activator N-acetyl-L-glutamate displaces the equilibrium towards monomer formation Rattus norvegicus

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.4.16
-
 Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.16 ATP + NH4+ + CO2 + H2O
-
 Rattus norvegicus ADP + phosphate + carbamoylphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.4.16 monomer 1 * 160000, sedimentation velocity measurement in presence of acetylglutamate alone, enzyme exists in a rapid, reversible monomer-dimer equilibrium. In presence of all substrates the enzyme exists as a monomer. The activator N-acetyl-L-glutamate displaces the equilibrium towards monomer formation Rattus norvegicus