EC Number   |
Reaction |
Reference |
|---|
    2.1.3.2 | carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate |
allosteric enzyme, in absence of effectors, two-state, concerted transition model |
662646 |
| 2.1.3.2 | carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate |
ATCase follows an ordered Bi Bi reaction mechanism in which carbamoyl phosphate must bind before L-aspartate and the product N-carbamoyl-L-aspartate leaves the active site before inorganic phosphate |
718699 |
| 2.1.3.2 | carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate |
catalytic and regulatory mechanisms, overview. The enzyme undergoes as it shifts between its low-activity, low-affinity form, T state, to its high-activity, high-affinity form, R state, and allosteric effectors modulate the activity. The ATCase-catalyzed reaction is regulated by nucleotide binding some 60 A from the active site, inducing structural alterations that modulate catalytic activity. The catalytic mechanism is ordered, carbamoyl phosphate binds before aspartate, and carbamoyl aspartate leaves before phosphate. Cooperativity is induced by aspartate binding |
718458 |
| 2.1.3.2 | carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate |
cooperative mechanism of substrate binding |
661693 |
| 2.1.3.2 | carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate |
enzyme exhibits homotropic cooperativity for aspartate, is heterotropically activated by ATP and is heterotropically inhibited by CTP and UTP |
485838, 485872 |
| 2.1.3.2 | carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate |
kinetic data suggest an ordered bi bi mechanism |
485863 |
| 2.1.3.2 | carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate |
ordered substrate binding with induced fit |
663253 |
| 2.1.3.2 | carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate |
reaction mechanism |
485837, 485838, 485856, 485857, 485858, 485861, 485863 |
| 2.1.3.2 | carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate |
reaction proceeds via a nucleophilic attack by the free amino group of L-aspartate on the carbon of carbamoylphosphate |
485843 |
| 2.1.3.2 | carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate |
significant role of protein-solvent interactions in regulatory conformational changes |
661450 |
