EC Number   |
Subunits |
Reference  |
|---|
    6.3.4.2 | ? |
x * 56180, calculation from nucleotide sequence |
648966 |
| 6.3.4.2 | ? |
x * 64622, calculation from nucleotide sequence |
648966 |
| 6.3.4.2 | ? |
x * 64783, calculation from nucleotide sequence |
648966 |
| 6.3.4.2 | ? |
x * 65514, calculation from nucleotide sequence |
648966 |
| 6.3.4.2 | ? |
x * 65678, calculation from nucleotide sequence |
648966 |
| 6.3.4.2 | ? |
x * 66705,calculation from nucleotide sequence |
648966 |
| 6.3.4.2 | ? |
x * 66710, calculation from nucleotide sequence |
648966 |
| 6.3.4.2 | tetramer |
- |
648968 |
| 6.3.4.2 | tetramer |
the enzyme exists as an inactive dimer in the absence of ATP and UTP. In the presence of saturating concentrations of ATP and UTP, the CTP synthetase protein exists as an active tetramer. Increasing concentrations of ATP and UTP cause a dose-dependent conversion of the dimeric species to a tetramer. Tetramerization is dependent on UTP and Mg2+ ions. ATP facilitates the UTP-dependent teramerization of CTP synthetase by a mechanism that involves the ATP-dependent phosphorylation of UTP catalyzed by the enzyme |
648975 |
| 6.3.4.2 | tetramer |
2 * 60000 |
648977 |
