EC Number |
Reference |
---|
2.7.2.8 | - |
642361, 642363 |
2.7.2.8 | as complex with PII protein, NAGK binds Mg2+, ADP, arginine and N-acetylglutamate |
674874 |
2.7.2.8 | crystal structure of Maricaulis maris NAGS/K (mmNAGS/K) at 2.7 A resolution shows that it is a tetramer |
720845 |
2.7.2.8 | crystal structure of the complex between acetylglutamate kinase and PII of Synechococcus elongatus, at 2.75 A resolution |
689765 |
2.7.2.8 | crystal structures of both the DUF619 domain-lacking yNAGK, ligand-free as well as complexed with acetylglutamate or acetylglutamate and arginine, and of complete mature yNAGK are determined. yNAGK has as central structure a flat tetramer formed by two dimers of amino acid kinase domains |
723557 |
2.7.2.8 | crystal structures of EcNAGK free from substrates or complexed with the product N-acetyl-L-glutamyl-5-phosphate (NAGP) and with sulfate are determined at 2 A resolution. Structures reveal a novel, very open NAGK conformation to which substrates associate and from which roducts dissociate. In this conformation, the C-domain, which hosts most of the nucleotide site, rotates 24°-28° away from the N-domain, which hosts the acetylglutamate site, whereas the empty ATP site also exhibits some changes |
722965 |
2.7.2.8 | hanging drop vapor diffusion method at room temperature, crystal structure of a complex formed between two homotrimers of PII and a single hexamer of enzyme bound to the metabolites N-acetylglutamate, ADP, ATP, and arginine |
674874 |
2.7.2.8 | hanging-drop vapor diffusion method |
689895 |
2.7.2.8 | in complex with arginine |
675366 |
2.7.2.8 | in complex with MgADP-, N-acetyl-glutamte, AlF4-, with MgADP-, N-acetyl-glutamte, with ADp and SO42- |
642359 |