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Literature summary for 6.3.5.5 extracted from
- Carbamoyl-phosphate synthetase: an example of effects on enzyme properties of shifting an equilibrium between active monomer and active oligomer (1986), Biochemistry, 25, 5576-5582.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Orn | allosteric activation | Escherichia coli |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| UMP | allosteric inhibition | 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 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | reversible concentration-dependent self-association. When the enzyme concentration is lower than 0.01 g/L the enzyme exists as monomer under all conditions | Escherichia coli |
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