EC Number   |
Protein Variants |
Reference |
|---|
    6.3.4.2 | S568A |
2fold increase in Km value for UTP. Mutation of S568A significantly increases CTPS2 activity. The S568A mutation has a greater effect on the glutamine than ammonia-dependent activity |
715549 |
| 6.3.4.2 | S571A |
4fold increase in Km value for UTP |
715549 |
| 6.3.4.2 | G360A |
5fold increase in GTP-dependent activation of uncoupled glutamine hydrolysis compared to wild-type enzyme. Turnover number for NH4Cl-dependent GTP synthesis reaction is 1.2fold higher than wild-type value |
661713 |
| 6.3.4.2 | G110A |
affinity of the mutant enzyme for GTP is reduced 2-4fold, enzyme exhibits wild-type NH3-dependent activity and affinity for glutamine, but impaired glutamine-dependent CTP formation |
648962 |
| 6.3.4.2 | S330A |
CTP synthetase activity in cells bearing the mutant enzyme is elevated, mutation causes an elevation in the Vmax of the reaction. Mutation does not have a major effect on the oligomerization of CTP synthetase |
648973 |
| 6.3.4.2 | S36A |
CTP synthetase activity in extracts from cells bearing the mutant enzyme is reduced when compared with cells bearing the wild-type enzyme, decrease in Vmax of the reaction. The amount of inactive dimeric enzyme form is 54% greater compared to wild-type enzyme |
648973 |
| 6.3.4.2 | S354A |
CTP synthetase activity in extracts from cells bearing the mutant enzyme is reduced when compared with cells bearing the wild-type enzyme, decrease in Vmax of the reaction. The amount of inactive dimeric enzyme form is 98% greater compared to wild-type enzyme |
648973 |
| 6.3.4.2 | S454A |
CTP synthetase activity in extracts from cells bearing the mutant enzyme is reduced when compared with cells bearing the wild-type enzyme. Mutation does not have a major effect on the oligomerization of CTP synthetase |
648973 |
| 6.3.4.2 | more |
deletion of the C-terminal regulatory domain, residues Ser562-Asp591, of CTPS1 greatly increases the Vmax of the enzyme |
715549 |
| 6.3.4.2 | DELTA20 |
deletion of the N-terminal 20 amino acids alone is sufficient to disrupt cytoophidium assembly, mutant protein forms distinct cytoplasmic structures which appear as large clusters |
744847 |
