Cloned (Comment) | Organism |
---|---|
- |
Photinus pyralis |
Protein Variants | Comment | Organism |
---|---|---|
H461D | relative specific activity is 57.6% as compared to wild-type enzyme. Mutation decreases ATP binding affinity, reduces the melting temperature of protein by around 25°C and shifts its optimum temperature of activity to 10°C | Photinus pyralis |
H489D | relative specific activity is 112% as compared to wild-type enzyme. Mutation introduces a new salt bridge between the C-terminal and N-terminal domains and increases protein rigidity but only slightly improves its thermal stability | Photinus pyralis |
H489K | relative specific activity is 115% as compared to wild-type enzyme. Mutation increases protein rigidity but only slightly improves its thermal stability | Photinus pyralis |
H489M | relative specific activity is 103% as compared to wild-type enzyme | Photinus pyralis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.002 | - |
D-firefly luciferin | pH 7.8, temperature not specified in the publication, mutant enzyme H489K | Photinus pyralis | |
0.0023 | - |
D-firefly luciferin | pH 7.8, temperature not specified in the publication, mutant enzyme H489M | Photinus pyralis | |
0.0025 | - |
D-firefly luciferin | pH 7.8, temperature not specified in the publication, mutant enzyme H489D | Photinus pyralis | |
0.005 | - |
D-firefly luciferin | pH 7.8, temperature not specified in the publication, mutant enzyme H461D | Photinus pyralis | |
0.005 | - |
D-firefly luciferin | pH 7.8, temperature not specified in the publication, wild-type enzyme | Photinus pyralis | |
0.04 | - |
ATP | pH 7.8, temperature not specified in the publication, mutant enzyme H489M | Photinus pyralis | |
0.06 | - |
ATP | pH 7.8, temperature not specified in the publication, mutant enzyme H489K | Photinus pyralis | |
0.06 | - |
ATP | pH 7.8, temperature not specified in the publication, wild-type enzyme | Photinus pyralis | |
0.09 | - |
ATP | pH 7.8, temperature not specified in the publication, mutant enzyme H489D | Photinus pyralis | |
0.1 | - |
ATP | pH 7.8, temperature not specified in the publication, mutant enzyme H461D | Photinus pyralis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-firefly luciferin + O2 + ATP | Photinus pyralis | - |
firefly oxyluciferin + CO2 + AMP + diphosphate + hv | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Photinus pyralis | P08659 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Photinus pyralis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-firefly luciferin + O2 + ATP | - |
Photinus pyralis | firefly oxyluciferin + CO2 + AMP + diphosphate + hv | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
10 | - |
mutant enzyme H461D | Photinus pyralis |
20 | - |
mutant enzyme H489M | Photinus pyralis |
25 | - |
wild-type enzyme | Photinus pyralis |
25 | - |
mutant enzyme H489D | Photinus pyralis |
30 | - |
mutant enzyme H489K | Photinus pyralis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
t1/2: 17 min (wild-type enzyme), 9.5 min (mutant enzyme H461D), 12.6 min (mutant enzyme H489K), 20.2 min (mutant enzyme H489D) and 24.4 min (mutant enzyme H489M) | Photinus pyralis |
30 | - |
t1/2: 10.5 min (wild-type enzyme), 6.9 min (mutant enzyme H461D), 8.3 min (mutant enzyme H489K), 11.1 min (mutant enzyme H489D) and 9.5 min (mutant enzyme H489M) | Photinus pyralis |
35 | - |
t1/2: 6.1 min (wild-type enzyme), 3.7 min (mutant enzyme H461D), 6.4 min (mutant enzyme H489K), 6.5 min (mutant enzyme H489D) and 5.7 min (mutant enzyme H489M) | Photinus pyralis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
wild-type enzyme, mutant enzymes H461D, H489K, H489D and H489M | Photinus pyralis |