EC 1.13.12.18 - Dinoflagellate luciferase

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IntEnz Enzyme Nomenclature
EC 1.13.12.18

Names

Accepted name:
dinoflagellate luciferase
Other names:
(dinoflagellate luciferin) luciferase
Gonyaulax luciferase
Systematic name:
Gonyaulax-luciferin:oxygen 132-oxidoreductase

Reaction

Comments:

A luciferase from dinoflagelates such as Gonyaulax polyhedra, 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

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Dunlap, J. C., Hastings, J. W.
    The biological clock in Gonyaulax controls luciferase activity by regulating turnover.
    J. Biol. Chem. 256: 10509-10518 (1981). [PMID: 7197271]
  2. Morse, D., Pappenheimer, A. M., Hastings, J. W.
    Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyhedra.
    J. Biol. Chem. 264: 11822-11826 (1989). [PMID: 2745419]
  3. Bae, Y. M., Hastings, J. W.
    Cloning, sequencing and expression of dinoflagellate luciferase DNA from a marine alga, Gonyaulax polyhedra.
    Biochim. Biophys. Acta 1219: 449-456 (1994). [PMID: 7918642]
  4. Li, L.
    Gonyaulax luciferase: gene structure, protein expression, and purification from recombinant sources.
    Meth. Enzymol. 305: 249-258 (2000). [PMID: 10812605]
  5. Morse, D., Mittag, M.
    Dinoflagellate luciferin-binding protein.
    Meth. Enzymol. 305: 258-276 (2000). [PMID: 10812606]
  6. Schultz, L. W., Liu, L., Cegielski, M., Hastings, J. W.
    Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole.
    Proc. Natl. Acad. Sci. USA 102: 1378-1383 (2005). [PMID: 15665092]

[EC 1.13.12.18 created 2011]