1.13.12.24: calcium-regulated photoprotein
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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
ECTree
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General Information
General Information on EC 1.13.12.24 - calcium-regulated photoprotein
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physiological function
protein-protein energy transfer between green fluoresecent protein and aequorin, possibly involving a Forster-type mechanism in vivo as well as in vitro
physiological function
when calcium binds at either or both EF hands I and IV the helices of these hands will change their relative orientations. Displacement of the helices flanking the C-terminal loop would disrupt the hydrogen-bonding network of the loop, resulting in a relocation of the side chain of Tyr 184. This would disrupt the hydrogen bonds to His 169 and the peroxide. The peroxide would be free to attack the adjacent carbonylic C3 to initiate the light-emitting reaction. The C-terminal tail could become partly or completely uncoupled from the helices, opening up the ligand-binding site to permit the egress of one or both reaction products
physiological function
the enzyme is responsible for the bioluminescence of the ctenophore Beroe abyssicola