Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate | using an elastic network model representation a normal mode analysis shows that the conformational mechanisms for substrate binding by NAGK strongly correlate with the intrinsic dynamics of the enzyme in the unbound form. The conformational change observed between the open and closed forms of EcNAGK are essentially accomplished by movements along a small subset of modes | Escherichia coli |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
EcNAGK | - |
Escherichia coli |