Crystallization (Comment) | Organism |
---|---|
development of a structural model of human enzyme that is fully consistent with the functional effects of the 14 missense mutations that have been identified in N-acetylglutamate synthase-deficient patients | Homo sapiens |
to 2.7 A resolution. Enzyme is a tetramer. Each subunit has an amino acid kinase domain, which is likely responsible for N-acetylglutamate kinase activity and has a putative arginine binding site, and an N-acetyltransferase domain that contains the putative N-acetylglutamate synthase active site. The angle of rotation between amino acid kinase and N-acetyltransferase domains varies among crystal forms and subunits within the tetramer. A rotation of 26° is sufficient to close the predicted AcCoA binding site, thus reducing enzymatic activity | Maricaulis maris |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-arginine | allosteric inhibition | Homo sapiens | |
L-arginine | allosteric inhibition | Maricaulis maris |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
bifunctional N-acetylglutamate synthase/kinase | - |
Maricaulis maris | Q0ASS9 | bifunctional N-acetylglutamate synthase/kinase | - |
Subunits | Comment | Organism |
---|---|---|
tetramer | crystallization data | Homo sapiens |
tetramer | crystallization data | Maricaulis maris |
Synonyms | Comment | Organism |
---|---|---|
NAGS/K | - |
Homo sapiens |
NAGS/K | - |
Maricaulis maris |