Activating Compound | Comment | Organism | Structure |
---|---|---|---|
L-arginine | slight activation is observed at 1 mM L-arginine | Maricaulis maris |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | Maricaulis maris |
Crystallization (Comment) | Organism |
---|---|
crystal structure of Maricaulis maris NAGS/K (mmNAGS/K) at 2.7 A resolution shows that it is a tetramer | Maricaulis maris |
Protein Variants | Comment | Organism |
---|---|---|
I106M | to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A | Maricaulis maris |
I294M | to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A | Maricaulis maris |
L367M | to increase phasing power, three additional amino acids codons are mutated to methionine (I106M, I294M and L367M). Crystals from this mutant protein are diffracted to 2.7 A | Maricaulis maris |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Maricaulis maris | - |
- |
- |
Purification (Comment) | Organism |
---|---|
using Ni-NTA chromatography | Maricaulis maris |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
20.1 | - |
pH 7.4, 37°C | Maricaulis maris |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + N-acetyl-L-glutamate | - |
Maricaulis maris | ADP + N-acetyl-L-glutamate 5-phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | crystal structure | Maricaulis maris |
Synonyms | Comment | Organism |
---|---|---|
NAGS-K | enzyme has both N-acetylglutamate synthase and kinases activity | Maricaulis maris |