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Literature summary for 1.13.12.7 extracted from
- Bifunctional role of leucine 300 of firefly luciferase in structural rigidity (2017), Int. J. Biol. Macromol., 101, 67-74 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Lampyris turkestanicus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| L300E | specific activity is increased and Km-value is increased about 1.7fold compared with the wild-type enzyme | Lampyris turkestanicus |
| L300K | relative stability of mutant luciferase increases compared with native luciferase, mutation causes no effects on bioluminescence spectrum | Lampyris turkestanicus |
| L300R | relative stability of mutant luciferase increases compared with native luciferase, mutation causes no effects on bioluminescence spectrum, specific activity is increased as compared to wild-type enzyme | Lampyris turkestanicus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 10 | - |
D-firefly luciferin | pH and temperature not specified in the publication, mutant enzyme L300K | Lampyris turkestanicus |  |
| 12.5 | - |
D-firefly luciferin | pH and temperature not specified in the publication, wild-type enzyme | Lampyris turkestanicus | |
| 14 | - |
D-firefly luciferin | pH and temperature not specified in the publication, mutant enzyme L300R | Lampyris turkestanicus | |
| 25 | - |
D-firefly luciferin | pH and temperature not specified in the publication, mutant enzyme L300E | Lampyris turkestanicus | |
| 83 | - |
ATP | pH and temperature not specified in the publication, wild-type enzyme | Lampyris turkestanicus | |
| 88 | - |
ATP | pH and temperature not specified in the publication, mutant enzyme L300K | Lampyris turkestanicus | |
| 100 | - |
ATP | pH and temperature not specified in the publication, mutant enzyme L300R | Lampyris turkestanicus | |
| 140 | - |
ATP | pH and temperature not specified in the publication, mutant enzyme L300E | Lampyris turkestanicus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-firefly luciferin + O2 + ATP | Lampyris turkestanicus | - |
firefly oxyluciferin + CO2 + AMP + diphosphate + hv | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lampyris turkestanicus | Q5UFR2 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Lampyris turkestanicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-firefly luciferin + O2 + ATP | - |
Lampyris turkestanicus | firefly oxyluciferin + CO2 + AMP + diphosphate + hv | - |
? | |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
wild-type enzyme, mutant enzyme L300K and mutant enzyme L300E | Lampyris turkestanicus |
| 30 | - |
mutant enzyme L300R | Lampyris turkestanicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
wild-type enzyme, mutant enzyme L300K, mutant enzyme L300E and mutant enzyme L300R | Lampyris turkestanicus |
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