EC Number   |
Inhibitors |
Structure |
|---|
    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 |
   |
| 2.7.2.8 | trichloroacetic acid |
complete inactivation at 30% |
|
| 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 | 2-oxoglutarate |
complete inhibition at 0.5 mM |
|
| 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 | arginine |
enzyme has no allosteric properties and its activity is influenced neither by arginine nor by any of the intermediates of the arginine biosynthetic pathway |
|
| 2.7.2.8 | arginine |
feedback inhibition |
|
| 2.7.2.8 | arginine |
feedback inhibition is markedly dependent on pH, above pH 9 no inhibition |
|
| 2.7.2.8 | L-arginine |
feedback inhibition, almost complete inhibition at 10 mM |
|
| 2.7.2.8 | L-arginine |
feedback inhibition. SYPA5-5 N-acetylglutamate kinase feedback inhibition by L-arginine can be deregulated by introducing point mutations, H268N or R209A |
|
