1.13.12.6: Cypridina-luciferin 2-monooxygenase
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For detailed information about Cypridina-luciferin 2-monooxygenase, go to the full flat file.
Word Map on EC 1.13.12.6
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1.13.12.6
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bioluminescence
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luminescence
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hilgendorfii
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luciferases
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ostracod
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firefly
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analysis
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gaussia
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diagnostics
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molecular biology
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biotechnology
- 1.13.12.6
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bioluminescence
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luminescence
- hilgendorfii
- luciferases
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ostracod
- firefly
- analysis
- gaussia
- diagnostics
- molecular biology
- biotechnology
Reaction
Synonyms
Apogon luciferase, Apogon luciferase 1, CLase, CLuc, Cypridina luciferase, Cypridina luciferin 2-monooxygenase, Cypridina noctiluca luciferase, Cypridina-type luciferase, Fbp, FBP-IgG, luciferase (Cypridina luciferin), PGE2-luciferase, Vargula luciferase
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General Information
General Information on EC 1.13.12.6 - Cypridina-luciferin 2-monooxygenase
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evolution
malfunction
Producibility and relative specific activity are apparently reduced in Cluc mutated in the phosphorylation sites, although the thermostability and secretion efficiency are not affected. Defects in the glycosylation modification are not related to secretion process and stability of the protein
physiological function
the enzyme enables Cypridina luciferin to emit light efficiently through an oxidation reaction
Parapriacanthus ransonneti, a bioluminescent fish, obtains not only its luciferin but also its luciferase enzyme from bioluminescent ostracod prey. Experiments where fish are fed with Vargula hilgendorfii, demonstrate the specific uptake of the luciferase to the fish's light organs. This kleptoprotein system allows an organism to use novel functional proteins that are not encoded in its genome and provides an evolutionary alternative to DNA-based molecular evolution
evolution
Parapriacanthus ransonneti, a bioluminescent fish, obtains not only its luciferin but also its luciferase enzyme from bioluminescent ostracod prey. The enzyme purified from the fish's light organs is identical to the luciferase of Cypridina noctiluca, a bioluminescent ostracod that they feed upon. This kleptoprotein system allows an organism to use novel functional proteins that are not encoded in its genome and provides an evolutionary alternative to DNA-based molecular evolution