EC Number | Cloned (Comment) | Organism |
---|---|---|
1.13.12.7 | recombinant expression of the chimeric mutant luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase in HEK-293 cells and in Escherichia coli strain BL21(DE3)pLysS | Photinus pyralis |
1.13.12.7 | recombinant expression of the chimeric mutant luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase in HEK-293 cells and in Escherichia coli strain BL21(DE3)pLysS | Luciola italica |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.13.12.7 | additional information | construction of a chimeric enzyme luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme shows 2fold enhanced activity and 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. Further engineering to enhance thermal and pH stability produces a different luciferase called PLG2, that shows 4.4fold enhanced activity and 2.2fold greater bioluminescence quantum yield compared to the wild-type. Five amino acid changes based on Luciola italica are the main determinants of the improved bioluminescence properties | Luciola italica |
1.13.12.7 | additional information | construction of a chimeric enzyme luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme shows 2fold enhanced activity and 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. Further engineering to enhance thermal and pH stability produces a different luciferase called PLG2, that shows 4.4fold enhanced activity and 2.2fold greater bioluminescence quantum yield compared to the wild-type. Five amino acid changes based on Luciola italica are the main determinants of the improved bioluminescence properties, comparison to the Photinus pyralis luciferase wild-type, overview | Photinus pyralis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.12.7 | D-firefly luciferin + O2 + ATP | Photinus pyralis | - |
firefly oxyluciferin + CO2 + AMP + diphosphate + hv | - |
? | |
1.13.12.7 | D-firefly luciferin + O2 + ATP | Luciola italica | - |
firefly oxyluciferin + CO2 + AMP + diphosphate + hv | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.12.7 | Luciola italica | Q1AG35 | - |
- |
1.13.12.7 | Photinus pyralis | P08659 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.12.7 | D-firefly luciferin + O2 + ATP | - |
Photinus pyralis | firefly oxyluciferin + CO2 + AMP + diphosphate + hv | - |
? | |
1.13.12.7 | D-firefly luciferin + O2 + ATP | - |
Luciola italica | firefly oxyluciferin + CO2 + AMP + diphosphate + hv | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.12.7 | firefly luciferase | - |
Photinus pyralis |
1.13.12.7 | Luciola italica luciferase | - |
Luciola italica |
1.13.12.7 | PpyWT | - |
Photinus pyralis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.13.12.7 | 37 | - |
assay at | Photinus pyralis |
1.13.12.7 | 37 | - |
assay at, mutants luc2 and PLG2 | Luciola italica |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.13.12.7 | 8 | - |
assay at | Photinus pyralis |
1.13.12.7 | 8 | - |
assay at, mutants luc2 and PLG2 | Luciola italica |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.13.12.7 | ATP | - |
Photinus pyralis | |
1.13.12.7 | ATP | - |
Luciola italica |