Application | Comment | Organism |
---|---|---|
analysis | due to the close phylogenetic relationship and similar biochemical properties of xanthomonad NAGS-K and mammalian NAGS the enzyme from Xanthomonas campestris could become a good model for mammalian NAGS in structural, biochemical and biophysical studies | Xanthomonas campestris |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Xanthomonas campestris |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NaCl | 200 mM NaCl inhibits the activity by about 22% | Xanthomonas campestris | |
Sodium acetate | 100 mM NaCl inhibits the activity by about 22% | Xanthomonas campestris |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.3 | - |
acetyl-CoA | 30°C, pH 9.0 | Xanthomonas campestris | |
2.8 | - |
L-glutamate | 30°C, pH 9.0 | Xanthomonas campestris |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Xanthomonas campestris | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Xanthomonas campestris |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
76.04 | - |
- |
Xanthomonas campestris |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + L-glutamate | no activity with D-glutamate and L-glutamine | Xanthomonas campestris | CoA + N-acetyl-L-glutamate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
NAGS-K | bifunctional N-acetylglutamate synthase and kinase | Xanthomonas campestris |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | - |
- |
Xanthomonas campestris |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
8.5 | 10 | pH 8.5: about 65% of maximal activity, pH 10.0: about 80% of maximal activity | Xanthomonas campestris |