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Literature summary extracted from
- Bioluminescent and structural features of native folded Gaussia luciferase (2018), J. Photochem. Photobiol. B, 183, 309-317 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.12.5 | KCl | substitution of NaCl by KCl does not significantly alter the dependence of light intensity on salt concentrations | Gaussia princeps |  |
| 1.13.12.5 | NaCl | maximum activity at 1.0-1.5 M, a high NaCl concentration enhances luciferase stability to thermal denaturation | Gaussia princeps | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.13.12.5 | expression in insect cells using a baculovirus expression system | Gaussia princeps |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.13.12.5 | 0.00214 | - |
coelenterazine | K0.5 value, Hill coefficient 1.8, pH 7.5, temperature not specified in the publication | Gaussia princeps | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.12.5 | Gaussia princeps | Q9BLZ2 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 1.13.12.5 | side-chain modification | enzyme contains five intramolecular S-S bonds per molecule | Gaussia princeps |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.13.12.5 | recombinant secreted enzyme | Gaussia princeps |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.13.12.5 | -20°C, 50% glycerol, stable for months | Gaussia princeps |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.12.5 | coelenterazine + O2 | - |
Gaussia princeps | ? + CO2 + hv | - |
? | |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.12.5 | 15 | 20 | - |
Gaussia princeps |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.12.5 | 1 | - |
30% residual activity | Gaussia princeps |
| 1.13.12.5 | 37 | - |
20% residual activity | Gaussia princeps |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.12.5 | 72 | - |
melting temperature | Gaussia princeps |
| 1.13.12.5 | 77 | - |
melting temperature, presence of 1 M NaCl | Gaussia princeps |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.12.5 | 7.5 | 8.5 | - |
Gaussia princeps |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.12.5 | 9 | - |
60% residual activity | Gaussia princeps |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.13.12.5 | metabolism | enzyme shows positive cooperativity with coelenterazine, rather due to the kinetic cooperativity conditioned by conformational changes in response to substrate binding than to the presence of two catalytic sites | Gaussia princeps |
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Release 2023.1 (January 2023)
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