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Literature summary for 1.13.12.24 extracted from
- Blue fluorescent protein from the calcium-sensitive photoprotein aequorin is a heat resistant enzyme, catalyzing the oxidation of coelenterazine (2004), FEBS Lett., 577, 105-110 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| dithiothreitol | in the presence of DTT, continuous luminescence is observed over 1 h. In the absence of DTT, the luminescence activity slowly decreases with a half period of 8.3 min | Aequorea victoria |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | treatment with excess EDTA leads to a shift in the blue fluorescence to a greenish fluorescence due to a non-covalent complex of apoaequorin with coelenteramide (oxyluciferin) in a molar ratio of 1:1. By incubation with coelenterazine in the absence of reducing reagents, the greenish fluorescent protein is converted to aequorin at 25°C | Aequorea victoria | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aequorea victoria | P02592 | - |
- |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 95 | - |
3 min, complete loss of activity. Fluorescence recovers to over 93% after incubating for a further 20 min at 24°C | Aequorea victoria |
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