EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.13.12.24 | [apoaequorin] + coelenterazine + O2 + 3 Ca2+ |
- |
Obelia longissima |
[excited state blue fluorescent protein] + CO2 |
- |
? |
| 1.13.12.24 | [apoaequorin] + coelenterazine + O2 + 3 Ca2+ |
- |
Mnemiopsis leidyi |
[excited state blue fluorescent protein] + CO2 |
- |
? |
| 1.13.12.24 | [apoaequorin] + coelenterazine + O2 + 3 Ca2+ |
- |
Obelia geniculata |
[excited state blue fluorescent protein] + CO2 |
- |
? |
| 1.13.12.24 | [apoaequorin] + coelenterazine + O2 + 3 Ca2+ |
- |
Clytia gregaria |
[excited state blue fluorescent protein] + CO2 |
- |
? |
| 1.13.12.24 | [apoaequorin] + coelenterazine + O2 + 3 Ca2+ |
- |
Mitrocoma cellularia |
[excited state blue fluorescent protein] + CO2 |
- |
? |
| 1.13.12.24 | [apoaequorin] + coelenterazine + O2 + 3 Ca2+ |
flash type light emission |
Aequorea victoria |
[excited state blue fluorescent protein] + CO2 |
- |
? |
| 1.13.12.24 | [apoaequorin] + coelenterazine + O2 + 3 Ca2+ |
the interaction between C-terminal Tyr208 and Tyr13 of the berovin first alpha-helix is essential for the stabilization and proper orientation of the 2-hydroperoxy adduct of coelenterazine within the internal cavity as well as for supporting its closed conformation. In contrast to hydromedusan photoproteins, in berovin the interplay between Tyr residues is conditioned rather by the pi-pi interaction of their phenyl rings than by the formation of hydrogen bonds between OH-groups |
Beroe abyssicola |
[excited state blue fluorescent protein] + CO2 |
- |
? |
| 1.13.12.24 | [apoaequorin] + coelenterazine + O2 + 3 Ca2+ |
the reaction mechanism of the bioluminescent protein mnemiopsin1 is revealed by X-ray crystallography and QM/MM simulations. A water molecule in the coelenteramide binding cavity is identified that forms a hydrogen bond with the amide nitrogen atom of coelenteramide, which, in turn, is hydrogen-bonded via another water molecule to Tyr-131. This observation supports the hypothesis that the function of the coelenteramide-bound water molecule is to catalyze the 2-hydroperoxycoelenterazine decarboxylation reaction by protonation of a dioxetanone anion, thereby triggering the bioluminescence reaction |
Mnemiopsis leidyi |
[excited state blue fluorescent protein] + CO2 |
- |
? |
| 1.13.12.24 | [apoaequorin] + coelenterazine + O2 + 3 Ca2+ |
the specific bioluminescence activities of five recombinant hydromedusan Ca2+-regulated photoproteins - aequorin, mitrocomin, clytin and obelins from Obelia longissima and Obelia geniculata is compared. Along with bioluminescence spectra, kinetics of light emission reactions and sensitivities to calcium, these photoproteins also differ in specific activities and consequently in quantum yields of biox02luminescent reactions. The highest specific activities are found for obelins and mitrocomin, whereas those of aequorin and clytin are lower |
Aequorea victoria |
[excited state blue fluorescent protein] + CO2 |
- |
? |
| 1.13.12.24 | [apoaequorin] + coelenterazine + O2 + 3 Ca2+ |
the specific bioluminescence activities of five recombinant hydromedusan Ca2+-regulated photoproteins - aequorin, mitrocomin, clytin and obelins from Obelia longissima and Obelia geniculata is compared. Along with bioluminescence spectra, kinetics of light emission reactions and sensitivities to calcium, these photoproteins also differ in specific activities and consequently in quantum yields of biox02luminescent reactions. The highest specific activities are found for obelins and mitrocomin, whereas those of aequorin and clytin are lower |
Obelia longissima |
[excited state blue fluorescent protein] + CO2 |
- |
? |
