General Stability | Organism |
---|---|
protective effects of osmolytes on the thermal denaturation and aggregation of arginine kinase from Euphausia superba: when the concentration of glycine, proline and glycerol increases, the relative activation is significantly enhanced, while the aggregation of the enzyme during thermal denaturation is decreased. The presence of these three osmolytes significantly decreases the tertiary structural changes of enzyme ESAK | Euphausia superba |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | 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 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme from muscle, 2.4fold by ammonium sulfate fractionation, gel filtration, affinity chromatography, and dialysis | Euphausia superba |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-arginine | - |
Euphausia superba | ADP + Nomega-phospho-L-arginine | - |
r |
Synonyms | Comment | Organism |
---|---|---|
ESAK | - |
Euphausia superba |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Euphausia superba |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
thermal denaturation directly induced ESAK aggregation, glycine, proline and glycerol not only prevent enzyme ESAK from inactivation and unfolding but also inhibit aggregation by stabilizing the enzyme conformation. Evaluation of the inactivation kinetics and rate constants, calculation of the transition free energy | Euphausia superba |
5 | 50 | purified enzyme, activity is relatively stable from 5°C to 23°C, but decreases rapidly from 25°C to 40°C. The activity is almost abolished at 50°C, half -life at 31.88°C | Euphausia superba |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Euphausia superba |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ADP | - |
Euphausia superba | |
ATP | - |
Euphausia superba |
General Information | Comment | Organism |
---|---|---|
additional information | enzyme structure homology modeling and docking simulations, overview | Euphausia superba |