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
-
photoproteins
-
bioluminescence
- aequorin
-
luminescence
- obelia
- longissima
- coelenteramide
-
ctenophore
-
coelenterate
-
jellyfish
-
ef-hand
- 2-hydroperoxycoelenterazine
- mnemiopsis
- hydroid
- clytin
-
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
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Metals Ions on EC 1.13.12.24 - calcium-regulated photoprotein
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
Mg2+
binding of Mg2+ to aequorin prevents the molecule from aggregating and stabilizes it in the monomeric form. Mg2+ binding induces conformational in the EF-hand loops. There are two Mg2+-binding sites, EF-hands I and III. EF-hand III binds to Mg2+ with higher affinity than EF-hand I, and only EF-hand III seems to be occupied by Mg2+ under physiological conditions
Ca2+
sequence displays three F-F hand structures that are characteristic for Ca2+-binding sites
Ca2+
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
Ca2+
when calcium binds at either or both EF hands I and IV the helices of these hands will change their relative orientations
