Reaction: dinoflagellate luciferin + O2 = oxidized dinoflagellate luciferin + H2O + hν
For diagram of reaction, click here
Glossary: dinoflagellate luciferin = (1S,2S,3S)-1-carboxy-3-(2-carboxyethyl)-12-ethyl-2,8,13,18-tetramethyl-17-vinyl-1,2,3,21-tetrahydro-5,7-ethanobilene-a-19(16H),52-dione
Other name(s): (dinoflagellate luciferin) luciferase; Gonyaulax luciferase
Systematic name: dinoflagellate-luciferin:oxygen 132-oxidoreductase
Comments: A luciferase from dinoflagellates such as Gonyaulax polyedra, Lingulodinium polyedrum, Noctiluca scintillans, and Pyrocystis lunula. It is a single protein with three luciferase domains. The luciferin is strongly bound by a luciferin binding protein above a pH of 7.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Dunlap, J.C. and Hastings, J.W. The biological clock in Gonyaulax controls luciferase activity by regulating turnover. J. Biol. Chem. 256 (1981) 10509-10518. [PMID: 7197271]
2. Morse, D., Pappenheimer, A.M., Jr. and Hastings, J.W. Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra. J. Biol. Chem. 264 (1989) 11822-11826. [PMID: 2745419]
3. Bae, Y.M. and Hastings, J.W. Cloning, sequencing and expression of dinoflagellate luciferase DNA from a marine alga, Gonyaulax polyedra. Biochim. Biophys. Acta 1219 (1994) 449-456. [PMID: 7918642]
4. Li, L. Gonyaulax luciferase: gene structure, protein expression, and purification from recombinant sources. Methods Enzymol. 305 (2000) 249-258. [PMID: 10812605]
5. Morse, D. and Mittag, M. Dinoflagellate luciferin-binding protein. Methods Enzymol. 305 (2000) 258-276. [PMID: 10812606]
6. Schultz, L.W., Liu, L., Cegielski, M. and Hastings, J.W. Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole. Proc. Natl. Acad. Sci. USA 102 (2005) 1378-1383. [PMID: 15665092]