Oplophorus-luciferin 2-monooxygenase
| Oplophorus-luciferin 2-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.13.12.13 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, an Oplophorus-luciferin 2-monooxygenase (EC 1.13.12.13) is a luciferase, an enzyme, from the deep-sea shrimp Oplophorus gracilirostris that catalyzes the chemical reaction:
- coelenterazine + O2 coelenteramide + CO2 + hν
Thus, the two substrates of this enzyme are the luciferin, Coelenterazine and O2, whereas its 3 products are the oxyluciferin, Coelenteramide, 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 Oplophorus-luciferin:oxygen 2-oxidoreductase (decarboxylating). This enzyme is also called Oplophorus luciferase.
References
- Shimomura O, Masugi T, Johnson FH, Haneda Y (1978). "Properties and reaction mechanism of the bioluminescence system of the deep-sea shrimp Oplophorus gracilorostris". Biochemistry. 17 (6): 994–8. doi:10.1021/bi00599a008. PMID 629957.
- Inouye S, Watanabe K, Nakamura H, Shimomura O (2000). "Secretional luciferase of the luminous shrimp Oplophorus gracilirostris: cDNA cloning of a novel imidazopyrazinone luciferase(1)". FEBS Lett. 481 (1): 19–25. doi:10.1016/S0014-5793(00)01963-3. PMID 10984608.