Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli BL21-DE3 cells | Amydetes vivianii |
Protein Variants | Comment | Organism |
---|---|---|
E270A | the mutation drastically decreases the spectral pH-sensitivity, and extends the activity profile above pH 9.0. These mutations also decrease the sensitivity to metals such as zinc, mercury and cadmium. The mutation may unwind a turn of the alpha-helix-10, indirectly increasing the interaction of the pH-sensor and other residues at the bottom of the luciferin binding site, stabilizing the green light emitting conformation | Amydetes vivianii |
E270G | the mutation drastically decreases the spectral pH-sensitivity, and extends the activity profile above pH 9.0. These mutations also decrease the sensitivity to metals such as zinc, mercury and cadmium. The mutation may unwind a turn of the alpha-helix-10, indirectly increasing the interaction of the pH-sensor and other residues at the bottom of the luciferin binding site, stabilizing the green light emitting conformation | Amydetes vivianii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0025 | - |
D-firefly luciferin | pH 8.0, 22°C, mutant enzyme E270A | Amydetes vivianii | |
0.004 | - |
D-firefly luciferin | pH 8.0, 22°C, mutant enzyme E270G | Amydetes vivianii | |
0.005 | - |
ATP | pH 8.0, 22°C, mutant enzyme E270A | Amydetes vivianii | |
0.009 | - |
ATP | pH 8.0, 22°C, wild-type enzyme | Amydetes vivianii | |
0.009 | - |
D-firefly luciferin | pH 8.0, 22°C, wild-type enzyme | Amydetes vivianii | |
0.017 | - |
ATP | pH 8.0, 22°C, mutant enzyme E270G | Amydetes vivianii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-firefly luciferin + O2 + ATP | Amydetes vivianii | - |
firefly oxyluciferin + CO2 + AMP + diphosphate + hv | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Amydetes vivianii | A0A3F2YLV6 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-firefly luciferin + O2 + ATP | - |
Amydetes vivianii | firefly oxyluciferin + CO2 + AMP + diphosphate + hv | - |
? | |
D-firefly luciferin + O2 + ATP | the enzyme display a typical change in bioluminescence color to red at acidic pH, high temperatures and in the presence of heavy metals | Amydetes vivianii | firefly oxyluciferin + CO2 + AMP + diphosphate + hv | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at | Amydetes vivianii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
ATP | kinetic properties of luciferase and E270 mutants | Amydetes vivianii | |
additional information | - |
D-firefly luciferin | kinetic properties of luciferase and E270 mutants | Amydetes vivianii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Amydetes vivianii |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
ATP | kinetic properties of luciferase and E270 mutants | Amydetes vivianii | |
additional information | - |
D-firefly luciferin | kinetic properties of luciferase and E270 mutants | Amydetes vivianii |