Cypridina-luciferin 2-monooxygenase
In enzymology, a Cypridina-luciferin 2-monooxygenase (EC 1.13.12.6) is an enzyme that catalyzes the chemical reaction
- Cypridina luciferin + O2 oxidized Cypridina luciferin + CO2 + hnu
Thus, the two substrates of this enzyme are Cypridina luciferin and O2, whereas its 3 products are oxidized Cypridina luciferin, CO2, and light.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O with incorporation of one atom of oxygen (internal monooxygenases o internal mixed-function oxidases). The systematic name of this enzyme class is Cypridina-luciferin:oxygen 2-oxidoreductase (decarboxylating). Other names in common use include Cypridina-type luciferase, luciferase (Cypridina luciferin), and Cypridina luciferase.
The primary sequence was determined by cloning the cDNA.[1]
References
- Cormier MJ, Crane JM Jr, Nakano Y (1967). "Evidence for the identity of the luminescent systems of Porichthys porosissimus (fish) and Cypridina hilgendorfii (crustacean)". Biochem. Biophys. Res. Commun. 29 (5): 747–52. doi:10.1016/0006-291X(67)90281-1. PMID 5624784.
- Karpetsky TP and White EH (1973). "The synthesis of Cypridina etioluciferamine and the proof of the structure of Cypridina luciferin". Tetrahedron 29 (23): 3761–3773. doi:10.1016/0040-4020(73)80193-0.
- Kishi Y, Goto, T, Hirata Y, Shiromura O and Johnson FH (1966). "Cypridina bioluminescence. I. Structure of Cypridina luciferin". Tetrahedron Lett. 7: 3427–3436. doi:10.1016/S0040-4039(01)82806-9.
- Tsuji FI, Lynch RV 3rd Stevens CL (1974). "Some properties of luciferase from the bioluminescent crustacean, Cypridina hilgendorfii". Biochemistry. 13 (25): 5204–9. doi:10.1021/bi00722a024. PMID 4433517.
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