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Literature summary for 6.3.4.2 extracted from
- Steady-state kinetics of the glutaminase reaction of CTP synthase from Lactococcus lactis. The role of the allosteric activator GTP incoupling between glutamine hydrolysis and CTP synthesis (2002), Eur. J. Biochem., 269, 4772-4779.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| GTP | the binding of GTP to the allosteric site promotes coordination of the phosphorylation of UTP and hydrolysis of glutamine for optimal efficiency in CTP synthesis rather than just acting to increase the rate of glutamine hydrolysis itself | Lactococcus lactis |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| adenosine 5'-[beta,gamma-imido]triphosphate | poor inhibitor compared to ATPgammaS | Lactococcus lactis | |
| ATPgammaS | - |
Lactococcus lactis | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lactococcus lactis | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + UTP + glutamine | - |
Lactococcus lactis | ADP + phosphate + CTP + Glu | - |
? | |
| ATP + UTP + NH4+ | - |
Lactococcus lactis | ADP + phosphate + CTP | - |
? | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Lactococcus lactis |
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