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Literature summary extracted from

  • Kim, J.; Raushel, F.M.
    Allosteric control of the oligomerization of carbamoyl phosphate synthetase from Escherichia coli (2001), Biochemistry, 40, 11030-11036.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.5.5 IMP the effector stabilzes the (alpha,beta)4-tetramer of enzyme Escherichia coli
6.3.5.5 L-ornithine the effector stabilizes the (alpha,beta)4-tetramer of enzyme Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.5.5 L421E mutant forms a (alpha/beta)2-dimer in presence of ornithine, IMP and UMP Escherichia coli
6.3.5.5 L421E/N987D no oligomerization Escherichia coli
6.3.5.5 N987D mutant forms a (alpha/beta)-monomer regardless of the presence of any allosteric effectors Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.5 UMP the inhibitor stabilizes the (alpha,beta)2-dimer of enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.5.5 0.038
-
 ATP pH 7.6, wild-type enzyme in presence of ornithine and in comparison to mutant enzymes Escherichia coli
6.3.5.5 0.37
-
 ATP pH 7.6, wild-type enzyme in presence of IMP and in comparison to mutant enzymes Escherichia coli
6.3.5.5 0.47
-
 ATP pH 7.6, wild-type enzyme in absence of effectors and in comparison to mutant enzymes Escherichia coli
6.3.5.5 1.6
-
 ATP pH 7.6, wild-type enzyme in presence of UMP and in comparison to mutant enzymes Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.5.5 42000
-
 alpha,beta, 1 * 42000 + 1 * 118000, the effectors ornithine, IMP and UMP modulate the oligomerization of the heterodimer to higher ordered species Escherichia coli
6.3.5.5 118000
-
 alpha,beta, 1 * 42000 + 1 * 118000, the effectors ornithine, IMP and UMP modulate the oligomerization of the heterodimer to higher ordered species Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.5.5 2 ATP + L-Gln + HCO3- Escherichia coli
-
 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.5 Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.5.5 additional information
-
 the catalytic activity is dependent on the presence or absence of specific allosteric ligands but independent of the oligomeric state of the protein Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.5 2 ATP + L-Gln + HCO3-
-
 Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.5.5 heterodimer alpha,beta, 1 * 42000 + 1 * 118000, the effectors ornithine, IMP and UMP modulate the oligomerization of the heterodimer to higher ordered species Escherichia coli