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Literature summary for 6.3.4.2 extracted from
- Substrate inhibition of Lactococcus lactis cytidine 5'-triphosphate synthase by ammonium chloride is enhanced by salt-dependent tetramer dissociation (2003), Arch. Biochem. Biophys., 413, 17-22.
General Stability
| General Stability | Organism |
|---|---|
| the enzyme is stable in absence of ATP and UTP | Lactococcus lactis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| NH4Cl | substrate inhibition , a significant part of the inhibition can be shown to be due to the increase in ionic strength with increasing substrate concentrations | Lactococcus lactis |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 280000 | - |
tetramer, gel filtration | Lactococcus lactis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lactococcus lactis | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + UTP + NH4+ | - |
Lactococcus lactis | ADP + phosphate + CTP | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | - |
Lactococcus lactis |
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