EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.3.1 | - |
Helicobacter pylori |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.3.1 | C66A | residue involved in disulfide bond. Catalytic turnover and the catalytic efficiency for the mutant proteins similar to the wild-type | Helicobacter pylori |
3.5.3.1 | C73A | residue involved in disulfide bond. Catalytic turnover and the catalytic efficiency for the mutant proteins similar to the wild-type | Helicobacter pylori |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.5.3.1 | dithiothreitol | enzyme depleted of metal and reconstituted with Co2+, complete loss of activiy. Enzyme reconstitued with Mn2+, 20% loss of activity. Loss of catalytic activity in the wild-type protein with dithiothreitol is due to the interaction with Co2+ | Helicobacter pylori |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.3.1 | 5 | - |
L-arginine | mutant C73A, pH 7.2, 37°C | Helicobacter pylori | |
3.5.3.1 | 6 | - |
L-arginine | mutant C66A, pH 7.2, 37°C | Helicobacter pylori | |
3.5.3.1 | 6.2 | - |
L-arginine | wild-type, pH 7.2, 37°C | Helicobacter pylori |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.3.1 | Co2+ | enzyme is selective for Co2+ | Helicobacter pylori |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.3.1 | Helicobacter pylori | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.3.1 | L-arginine + H2O | - |
Helicobacter pylori | L-ornithine + urea | - |
? |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.3.1 | 62 | - |
melting temperature, mutants C73A and C66A depleted of Co2+ | Helicobacter pylori |
3.5.3.1 | 66 | - |
melting temperature, mutant C73A | Helicobacter pylori |
3.5.3.1 | 67 | - |
melting temperature, mutant C66A | Helicobacter pylori |
3.5.3.1 | 69 | - |
melting temperature, wild-type depleted of Co2+ | Helicobacter pylori |
3.5.3.1 | 71 | - |
melting temperature, wild-type | Helicobacter pylori |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.3.1 | 0.37 | - |
L-arginine | mutant C66A, pH 7.2, 37°C | Helicobacter pylori | |
3.5.3.1 | 0.52 | - |
L-arginine | wild-type, pH 7.2, 37°C | Helicobacter pylori | |
3.5.3.1 | 0.53 | - |
L-arginine | mutant C73A, pH 7.2, 37°C | Helicobacter pylori |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.3.1 | metabolism | the disulfide bond is important for the overall stability and folding of the protein. Mutant proteins lacking the disulfide bond start to unfold at lower temperature than the wild-type. In the mutant proteins, the Tm of the holoenzyme is 4°C higher than that of the apoenzyme indicating that in the absence of the disulfide bond the metal ions have relatively larger role in the stability of the mutant proteins compared to the wild-type | Helicobacter pylori |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.3.1 | 0.062 | - |
L-arginine | mutant C66A, pH 7.2, 37°C | Helicobacter pylori | |
3.5.3.1 | 0.084 | - |
L-arginine | wild-type, pH 7.2, 37°C | Helicobacter pylori | |
3.5.3.1 | 0.11 | - |
L-arginine | mutant C73A, pH 7.2, 37°C | Helicobacter pylori |