Cloned (Comment) | Organism |
---|---|
expressed as a fusion ptotein with an N-terminal polyHis tag in Escherichia coli and purified to homogeneity on a HisTrap column | Mus musculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.003 | - |
2-oxosuccinamate | pH 7.2, 30°C | Mus musculus | |
0.012 | - |
gamma-monomethyl-2-oxoglutaramate | pH 7.2, 30°C | Mus musculus | |
0.017 | - |
2-oxosuccinamate | pH 8.5, 30°C | Mus musculus | |
0.14 | - |
succinamate | pH 8.5, 30°C | Mus musculus | |
0.195 | - |
2-Oxoglutaramate | pH 8.5, 30°C | Mus musculus | |
0.23 | - |
succinamate | pH 7.2, 30°C | Mus musculus | |
1.27 | - |
Glutaramate | pH 8.5, 30°C | Mus musculus | |
1.48 | - |
Glutaramate | pH 7.2, 30°C | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
bioinformatic approaches are used to exploit bacterial operons to identify a putative omega-amidase by confirming this identification through characterization of the candidate protein | - |
Purification (Comment) | Organism |
---|---|
recombinant protein, purified to homogeneity on a HisTrap column | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-oxoglutaramate + H2O | tested at pH 7.2 and pH 8.5 | Mus musculus | 2-oxoglutarate + NH3 | - |
? | |
2-oxosuccinamate + H2O | tested at pH 7.2 and pH 8.5 | Mus musculus | oxaloacetate + NH3 | - |
? | |
gamma-monomethyl-2-oxoglutaramate + H2O | tested at pH 7.2 and pH 8.5 | Mus musculus | gamma-monomethyl-2-oxoglutarate + NH3 | - |
? | |
glutaramate + H2O | tested at pH 7.2 and pH 8.5 | Mus musculus | glutarate + NH3 | - |
? | |
additional information | L-glutamine and L-asparagine are no substrates at pH 7.2 and pH 8.5 | Mus musculus | ? | - |
? | |
succinamate + H2O | tested at pH 7.2 and pH 8.5 | Mus musculus | succinate + NH3 | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Mus musculus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.87 | - |
2-oxosuccinamate | pH 8.5, 30°C | Mus musculus | |
1.15 | - |
2-oxosuccinamate | pH 7.2, 30°C | Mus musculus | |
2 | - |
succinamate | pH 7.2, 30°C | Mus musculus | |
2.8 | - |
succinamate | pH 8.5, 30°C | Mus musculus | |
4.1 | - |
Glutaramate | pH 7.2, 30°C | Mus musculus | |
8.8 | - |
Glutaramate | pH 8.5, 30°C | Mus musculus | |
17.5 | - |
2-Oxoglutaramate | pH 8.5, 30°C | Mus musculus | |
134.5 | - |
gamma-monomethyl-2-oxoglutaramate | pH 7.2, 30°C | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
very low activity on 2-oxoglutaramte as substrate compared to assay at pH 8.5, presumably because Nit2 only acts on the linear forms of this substrate. The generation of the linear form from the predominant, cyclic form is pH-dependent, being much fatsre at pH 8.5 than at pH 7.2 | Mus musculus |
8.5 | - |
assay at | Mus musculus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.8 | - |
Glutaramate | pH 7.2, 30°C | Mus musculus | |
6.9 | - |
Glutaramate | pH 8.5, 30°C | Mus musculus | |
8.7 | - |
succinamate | pH 7.2, 30°C | Mus musculus | |
20 | - |
succinamate | pH 8.5, 30°C | Mus musculus | |
51.2 | - |
2-oxosuccinamate | pH 8.5, 30°C | Mus musculus | |
89.7 | - |
2-Oxoglutaramate | pH 8.5, 30°C | Mus musculus | |
385 | - |
2-oxosuccinamate | pH 7.2, 30°C | Mus musculus | |
11200 | - |
gamma-monomethyl-2-oxoglutaramate | pH 7.2, 30°C | Mus musculus |