1.13.12.24: calcium-regulated photoprotein
This is an abbreviated version!
For detailed information about calcium-regulated photoprotein, go to the full flat file.
Word Map on EC 1.13.12.24
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1.13.12.24
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photoproteins
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bioluminescence
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aequorin
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luminescence
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obelia
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longissima
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coelenteramide
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ctenophore
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coelenterate
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jellyfish
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ef-hand
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2-hydroperoxycoelenterazine
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mnemiopsis
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hydroid
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clytin
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hydromedusan
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leidyi
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synthesis
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analysis
- 1.13.12.24
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photoproteins
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bioluminescence
- aequorin
-
luminescence
- obelia
- longissima
- coelenteramide
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ctenophore
-
coelenterate
-
jellyfish
-
ef-hand
- 2-hydroperoxycoelenterazine
- mnemiopsis
- hydroid
- clytin
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hydromedusan
- leidyi
- synthesis
- analysis
Reaction
Synonyms
aequorin, alcium-activated photoprotein, berovin, BFP-aq, blue fluorescent protein, Ca2+-binding photoprotein, Ca2+-regulated photoprotein, clytin, halistaurin, mitrocomin, mnemiopsin, mnemiopsin 1, mnemiopsin 2, mnemiopsin1, obelin, phialidin
ECTree
1.13.12.24 calcium-regulated photoproteinAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.13.12.24 - calcium-regulated photoprotein
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[aequorin] 1,2-dioxetan-3-one
[aequorin] coelenteramide + CO2 + hnu
reaction in presence of Ca2+
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?
[apoaequorin] + coelenterazine + O2
[aequorin] 1,2-dioxetan-3-one
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-
-
?
[apoaequorin] + coelenterazine + O2
[apoaequorin] + coelenteramide + CO2 + hnu
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-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
[apoaequorin] + cp-coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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-
-
?
[apoaequorin] + f-coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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-
-
?
[apoaequorin] + h-coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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-
-
?
[apoaequorin] + hcp-coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
flash type light emission
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-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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
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-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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
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-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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
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-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
-
-
-
?
[apoaequorin] + coelenterazine + O2 + 3 Ca2+
[excited state blue fluorescent protein] + CO2
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
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-
?
additional information
?
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aequorin exhibits an absorption near 454 nm. The native chromophore is Renilla luciferin or a nearly identical derivative. The binding of calcium ion to the photoprotein brings about a conformational change in the protein which results in the chromophore reacting with a protein side chain hydroperoxide to yield a protein bound luciferin hydroperoxide intermediate. This intermediate then decomposes to CO2 and an electronic excited state of the corresponding protein-oxyluciferin monoanion complex which leads to light emission
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?
additional information
?
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no substrates: bisdeoxycoelenterazine, C6-methoxycoelenterazine, e-coelenterazine
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-
?
additional information
?
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poor substrates: n-coelenterazine, bis-coelenterazine, methoxy-coelenterazine, e-coelenterazine
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?
additional information
?
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the luminescence peak of aequorin is found at 472 nm. In presence of high concentrations of green fluorescent protein, the peak shifts to 509 nm
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?
