Inhibitors | Comment | Organism | Structure |
---|---|---|---|
SDS | complete inactivation at 1.0 mM, the inactivation is a first-order reaction, with the kinetic processes shifting from a monophase to biphase as SDS concentrations increase. SDS concentrations lower than 5 mM do not induce conspicuous changes in tertiary structures, while higher concentrations of SDS exposedhydrophobic surfaces and induce conformational changes | Euphausia superba |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.3 | - |
L-arginine | pH 8.0, 20°C | Euphausia superba | |
0.47 | - |
ATP | pH 8.0, 20°C | Euphausia superba |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Euphausia superba |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
40000 | - |
1 * 40000 | Euphausia superba |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-arginine | Euphausia superba | - |
ADP + Nomega-phospho-L-arginine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Euphausia superba | W8GJF4 | from Antarctic krill | - |
Purification (Comment) | Organism |
---|---|
native enzyme from muscle, 2.4fold by ammonium sulfate fractionation, gel filtration, and affinity chromatography | Euphausia superba |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Euphausia superba | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1780 | - |
pH 8.0, 20°C, purified native enzyme from muscles | Euphausia superba |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-arginine | - |
Euphausia superba | ADP + Nomega-phospho-L-arginine | - |
r |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 40000 | Euphausia superba |
Synonyms | Comment | Organism |
---|---|---|
ATP: L-arginine phosphotransferase | - |
Euphausia superba |
ESAK | - |
Euphausia superba |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
- |
Euphausia superba |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
- |
60 | activity range, 50% activity at 0°C and 52°C, profile overview | Euphausia superba |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
84.8 | - |
L-arginine | pH 8.0, 20°C | Euphausia superba |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
- |
Euphausia superba |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 10 | activity range, profile overview | Euphausia superba |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Euphausia superba | |
ATP | - |
Euphausia superba |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.56 | - |
pH 8.0, 20°C | Euphausia superba | SDS |
General Information | Comment | Organism |
---|---|---|
additional information | the active region of enzyme AK is more flexible than the overall enzyme molecule | Euphausia superba |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
282.7 | - |
L-arginine | pH 8.0, 20°C | Euphausia superba |