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.

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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

ECTree

     1 Oxidoreductases

         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

             1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)

                1.13.12.6 Cypridina-luciferin 2-monooxygenase

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Results	in table
1	Activating Compound
5	AA Sequence
15	Application
1	CAS Registry Number
11	Cloned(Commentary)
4	General Information
2	General Stability
10	Inhibitors
10	KM Value [mM]
5	Localization
3	Metals/Ions
8	Molecular Weight [Da]
16	Natural Substrates/ Products (Substrates)
33	Organism
5	pH Optimum
1	pH Range
1	pI Value
3	Posttranslational Modification
16	Protein Variants
10	Purification (Commentary)
2	Reaction
3	Reaction Type
33	Reference
6	Source Tissue
1	Specific Activity [micromol/min/mg]
5	Storage Stability
31	Substrates and Products (Substrate)
6	Subunits
35	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
2	Temperature Stability [°C]
3	Turnover Number [1/s]

General Information

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General Information on EC 1.13.12.6 - Cypridina-luciferin 2-monooxygenase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

2 entries

malfunction

Cypridina noctiluca

Q75R40

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

745977

physiological function

Cypridina noctiluca

Q75R40

the enzyme enables Cypridina luciferin to emit light efficiently through an oxidation reaction

764911

evolution

Vargula hilgendorfii

P17554

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

765766

evolution

Cypridina noctiluca

Q75R40

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

765766