General Stability | Organism |
---|---|
inactivation at 1.3 M NaCl and KCl | Haloferax mediterranei |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
KCl | 1.3 M | Haloferax mediterranei | |
NaCl | 1.3 M | Haloferax mediterranei |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Haloferax mediterranei |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
32500 | - |
2 * 32500, SDS-PAGE | Haloferax mediterranei |
64200 | 68200 | gel filtration, PAGE, diffusion and sedimentation equilibrium | Haloferax mediterranei |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + 2-oxoglutarate | Haloferax mediterranei | - |
oxaloacetate + L-glutamate | - |
? | |
L-aspartate + 2-oxoglutarate | Haloferax mediterranei R-4 / ATCC 33500 | - |
oxaloacetate + L-glutamate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haloferax mediterranei | - |
- |
- |
Haloferax mediterranei R-4 / ATCC 33500 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Haloferax mediterranei |
Renatured (Comment) | Organism |
---|---|
thermal denaturation is not reversible | Haloferax mediterranei |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.53 | - |
purified enzyme | Haloferax mediterranei |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate + 2-oxoglutarate | - |
Haloferax mediterranei | oxaloacetate + L-glutamate | - |
? | |
L-aspartate + 2-oxoglutarate | - |
Haloferax mediterranei R-4 / ATCC 33500 | oxaloacetate + L-glutamate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 32500, SDS-PAGE | Haloferax mediterranei |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
65 | - |
3.5 M KCl | Haloferax mediterranei |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
thermal denaturation is not reversible, denaturation temperature of holoenzyme is 78.5°C | Haloferax mediterranei |
78.5 | - |
denaturation | Haloferax mediterranei |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | 7.9 | - |
Haloferax mediterranei |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | 2 mol of pyridoxal phosphate per mol of enzyme | Haloferax mediterranei | |
pyridoxal 5'-phosphate | a pyridoxal 5'-phosphate protein | Haloferax mediterranei |