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Literature summary for 6.3.5.5 extracted from

  • Pierrat, O.A.; Javid-Majd, F.; Raushel, F.M.
    Dissection of the conduit for allosteric control of carbamoyl phosphate synthetase by ornithine (2002), Arch. Biochem. Biophys., 400, 26-33.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
IMP allosteric effector Escherichia coli
L-ornithine positive allosteric activation, E783, T1042, and T1043 are primarily responsible for the binding of ornithine to enzyme Escherichia coli

Protein Variants

Protein Variants Comment Organism
E761A the residue is a key in the allosteric signal transduction pathway from ornithine to ATP Escherichia coli
E783A the allosteric activation of enzyme by ornithine is completely suppressed Escherichia coli
E783K the allosteric activation of enzyme by ornithine is completely suppressed Escherichia coli
E892A the allosteric activation of enzyme by ornithine is completely suppressed Escherichia coli
E892K the allosteric activation of enzyme by ornithine is completely suppressed Escherichia coli
additional information several mutations increase, reduce, suppresse, or reverse the allosteric effects of ornithine, UMP and IMP, the mutational analysis of ornithine, and potassium binding site strongly supports the proposal for a coupling between the allosteric transduction signal pathways for UMP,IMP and ornithine Escherichia coli
T1042K the residue is responsible for the binding of ornithine to enzyme Escherichia coli
T1043K the allosteric activation of enzyme by ornithine is completely suppressed Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
UMP
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
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
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information comparison of kcat in absence and presence of L-ornithine, UMP and IMP for wild-type and mutant enzymes Escherichia coli