Protein Variants | Comment | Organism |
---|---|---|
additional information | individual expression of the N-terminal domain, amino acid residues Y26-V362, and the C-terminal domain, amino acid residues K363-Q550. The domains fold independently and properly. The C-terminal domain, which contains the substrate-binding pocket, is completely inactive while the N-terminal domain with the two-metal-ion-centers and the core catalytic residues exhibits significant activity, especially towards substrates with activated phosphate bonds such as ATP, ADP, 4-nitrophenyl phosphate | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0129 | - |
5'-AMP | wild-type, pH 7.0, 22°C | Escherichia coli | |
0.0209 | - |
ATP | wild-type, pH 7.0, 22°C | Escherichia coli | |
0.0547 | - |
ADP | wild-type, pH 7.0, 22°C | Escherichia coli | |
5.713 | - |
4-nitrophenyl phosphate | wild-type, pH 7.0, 22°C | Escherichia coli | |
6.807 | - |
ATP | N-terminal protein domain, pH 7.0, 22°C | Escherichia coli | |
10.15 | - |
ADP | N-terminal protein domain, pH 7.0, 22°C | Escherichia coli | |
21.78 | - |
4-nitrophenyl phosphate | N-terminal protein domain, pH 7.0, 22°C | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Escherichia coli | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl phosphate + H2O | - |
Escherichia coli | 4-nitrophenol + phosphate | - |
? | |
5'-AMP + H2O | - |
Escherichia coli | adenosine + phosphate | - |
? | |
ADP + 2 H2O | - |
Escherichia coli | adenosine + 2 phosphate | - |
? | |
ATP + 3 H2O | - |
Escherichia coli | adenosine + 3 phosphate | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
36.5 | - |
ATP | N-terminal protein domain, pH 7.0, 22°C | Escherichia coli | |
40.8 | - |
4-nitrophenyl phosphate | wild-type, pH 7.0, 22°C | Escherichia coli | |
45.6 | - |
ADP | N-terminal protein domain, pH 7.0, 22°C | Escherichia coli | |
129 | - |
4-nitrophenyl phosphate | N-terminal protein domain, pH 7.0, 22°C | Escherichia coli | |
459.1 | - |
5'-AMP | wild-type, pH 7.0, 22°C | Escherichia coli | |
613.2 | - |
ADP | wild-type, pH 7.0, 22°C | Escherichia coli | |
757 | - |
ATP | wild-type, pH 7.0, 22°C | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | the two domains can be expressed individually in Escherichia coli and fold independently. The C-terminal domain, which contains the substrate-binding pocket, is completely inactive while the N-terminal domain with the two-metal-ion-centers and the core catalytic residues exhibits significant activity, especially towards substrates with activated phosphate bonds such as ATP, ADP, 4-nitrophenyl phosphate. The two domains do not reconstitute the full-length protein from the two folded individual domains | Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4.5 | - |
ADP | N-terminal protein domain, pH 7.0, 22°C | Escherichia coli | |
5.4 | - |
ATP | N-terminal protein domain, pH 7.0, 22°C | Escherichia coli | |
6.1 | - |
4-nitrophenyl phosphate | N-terminal protein domain, pH 7.0, 22°C | Escherichia coli | |
7.1 | - |
4-nitrophenyl phosphate | wild-type, pH 7.0, 22°C | Escherichia coli | |
11220 | - |
ADP | wild-type, pH 7.0, 22°C | Escherichia coli | |
35600 | - |
5'-AMP | wild-type, pH 7.0, 22°C | Escherichia coli | |
36200 | - |
ATP | wild-type, pH 7.0, 22°C | Escherichia coli |