EC Number   |
Inhibitors |
Structure |
|---|
    2.7.2.8 | arginine |
- |
   |
| 2.7.2.8 | ATP |
- |
|
| 2.7.2.8 | L-arginine |
pH and temperature dependent, sigmoidal dependence on concentration of arginine, Hill coefficient of 4, 1 mM, 37°C, 95% inhibition |
|
| 2.7.2.8 | L-arginine |
only for N-acetylglutamate synthase activity |
|
| 2.7.2.8 | L-arginine |
less inhibitory in the presence of the PII protein |
|
| 2.7.2.8 | L-arginine |
sigmoidal arginine inhibition kinetics, feedback inhibition, indentification of the N-terminal arginine site, mutational analysis, the mobile alphaH-beta16 loop of the arginine site is the modulatory signal receiver, overview |
|
| 2.7.2.8 | L-arginine |
- |
|
| 2.7.2.8 | L-arginine |
complete inhibition at 3-5 mM, PII-mediated relief from L-arginine inhibition is antagonized by 2-oxoglutarate |
|
| 2.7.2.8 | L-arginine |
complete inhibition at 0.1-1.0 mM, PII-mediated relief from L-arginine inhibition is antagonized by 2-oxoglutarate |
|
| 2.7.2.8 | L-arginine |
an allosteric inhibitor of mmNAGS/K, mechanism of allosteric inhibition of mmNAGS/K by L-arginine. L-Arginine is an allosteric inhibitor of NAGS/K but an allosteric activator of mammalian NAGS. In contrast to the structure of mmNAGS/K in the absence of L-arginine where there are conformational differences between the four subunits in the asymmetric unit, all four subunits in the L-arginine liganded structure have very similar conformations. In this conformation, the AcCoA binding site in the N-acetyltransferase domain is blocked by a loop from the amino acid kinase domain, as a result of a domain rotation that occurs when L-arginine binds |
|
