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Literature summary for 6.3.5.5 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
Search for more literature for 6.3.5.5

Activating Compound

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

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

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

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

Subunits

Subunits Comment Organism
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