Dinoflagellate luciferase

Dinoflagellate luciferase
Identifiers
EC number 1.13.12.18
CAS number 303183-71-3
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Dinoflagellate luciferase (EC 1.13.12.18, Gonyaulax luciferase) is a specific luciferase, an enzyme with systematic name dinoflagellate-luciferin:oxygen 132-oxidoreductase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

dinoflagellate luciferin + O2 \rightleftharpoons oxidized dinoflagellate luciferin + H2O + hnu

Dinoflagellate luciferase is a single protein with three luciferase domains.

References

  1. Dunlap, J.C. and Hastings, J.W. (1981). "The biological clock in Gonyaulax controls luciferase activity by regulating turnover". J. Biol. Chem. 256 (20): 10509–10518. PMID 7197271.
  2. Morse, D., Pappenheimer, A.M., Jr. and Hastings, J.W. (1989). "Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra". J. Biol. Chem. 264 (20): 11822–11826. PMID 2745419.
  3. Bae, Y.M. and Hastings, J.W. (1994). "Cloning, sequencing and expression of dinoflagellate luciferase DNA from a marine alga, Gonyaulax polyedra". Biochim. Biophys. Acta 1219 (2): 449–456. doi:10.1016/0167-4781(94)90071-x. PMID 7918642.
  4. Li, L. (2000). "Gonyaulax luciferase: gene structure, protein expression, and purification from recombinant sources". Methods Enzymol. 305: 249–258. doi:10.1016/s0076-6879(00)05492-6. PMID 10812605.
  5. Morse, D. and Mittag, M. (2000). "Dinoflagellate luciferin-binding protein". Methods Enzymol. 305: 258–276. doi:10.1016/s0076-6879(00)05493-8. PMID 10812606.
  6. Schultz, L.W., Liu, L., Cegielski, M. and Hastings, J.W. (2005). "Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole". Proc. Natl. Acad. Sci. USA 102: 1378–1383. doi:10.1073/pnas.0409335102. PMC 547824. PMID 15665092.

External links

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