EC Number   |
Protein Variants |
Reference |
|---|
    6.3.5.5 | A126M |
mutation in large subunit significantly decreases synthesis of carbamoyl phosphate without completely inactivating the enzyme |
662650 |
| 6.3.5.5 | A144Q |
mutant enzyme retains ATP specificity |
663332 |
| 6.3.5.5 | A182V |
reduced apparent affinity for HCO3-, sensitivity toward UMP is unchanched in comparison to wild-type enzyme |
652788 |
| 6.3.5.5 | A182V/S948F |
mutant is insensitive towards pyrimidine and purine nucleosides, activation by ornithine, although the affinity for this ligand is fivefold reduced in comparison to wild-type enzyme |
652788 |
| 6.3.5.5 | A23F |
migration of carbamate through the narrowest part of the carbamate tunnel is blocked. From the kinetic data the only reaction significantly affected by this mutation is the overall synthesis of carbamoyl phosphate (only 1.7% compared to wild-type) |
715279 |
| 6.3.5.5 | A23F |
mutant designed to block the migration of carbamate through the narrowest parts of the carbamate tunnel. Mutant retains 1.7% of the catalytic activity for the synthesis of carbamoyl phosphate relative to the wild type CPS |
715279 |
| 6.3.5.5 | A23K |
A23K mutation decreases the glutamine-dependent ATPase activity by an order of magnitude. While there is a decrease in the rate of carbamoyl phosphate formation, the enzyme utilizes two molecules of ATP for every molecule of carbamoyl phosphate synthesized |
715279 |
| 6.3.5.5 | A251C |
site-directed mutagenesis in the ammonia tunnel, analysis of secondary structure by circular dichroism measurements |
704173 |
| 6.3.5.5 | A309C |
kinetic properties are similar to those of the wild-type enzyme |
649964 |
| 6.3.5.5 | A309C/S35C |
kinetic properties are similar to those of the wild-type enzyme |
649964 |
