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Literature summary for 6.3.5.5 extracted from

  • Mora, P.; Rubio, V.; Cervera, J.
    Mechanism of oligomerization of Escherichia coli carbamoyl phosphate synthetase and modulation by the allosteric effectors. A site-directed mutagenesis study (2002), FEBS Lett., 511, 6-10.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ornithine
-
Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
H975L mutation abolishes oligomer formation even high enzyme concentrations or in the presence of ornithine Escherichia coli
H975L/N987V mutation abolishes oligomer formation even high enzyme concentrations or in the presence of ornithine Escherichia coli
L421E mutation prevents tetramer but not dimer formation Escherichia coli
L421E/H975L/N987V mutation abolishes oligomer formation even high enzyme concentrations or in the presence of ornithine Escherichia coli
L990A mutation abolishes oligomer formation even high enzyme concentrations or in the presence of ornithine Escherichia coli
N987V mutation decreases the oligomerisation Escherichia coli
N992A mutation abolishes oligomer formation even high enzyme concentrations or in the presence of ornithine Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
UMP
-
Escherichia coli

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
-
constant specific activity of wild-type enzyme irrespective of the enzyme concentration or of the elution position of the enzyme in the gel filtration system under conditions at which different oligomeric forms predominate 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
dimer at low concentrations in presence of UMP Escherichia coli
More in absence of effectors the enzyme behaves as a dissociating system possibly reflecting the dimer-tetramer equilibrium Escherichia coli
tetramer at high concentrations in presence of ornithine Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.004
-
UMP pH 8.0, 24°C Escherichia coli