Literature summary for 6.3.4.16 extracted from

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

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Activating Compound

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

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Rattus norvegicus

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
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

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Release 2023.1 (January 2023)