EC 1.13.12.7 - Firefly luciferase

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IntEnz Enzyme Nomenclature
EC 1.13.12.7

Names

Accepted name:
firefly luciferase
Other names:
Photinus pyralis luciferase
Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing)
firefly luciferin luciferase
luciferase (firefly luciferin)
luciferase
Photinus-luciferin 4-monooxygenase (ATP-hydrolysing)
Photinus-luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)
Systematic name:
D-firefly luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)

Reaction

Comments:

The enzyme, which is found in fireflies (Lampyridae), is responsible for their biolouminescence. The reaction begins with the formation of an acid anhydride between the carboxylic group of D-firefly luciferin and AMP, with the release of diphosphate. An oxygenation follows, with release of the AMP group and formation of a very short-lived peroxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO2 molecule. The spontaneous breakdown of the dioxetanone (rather than the hydrolysis of the adenylate) releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of oxyluciferin. The excited luciferin then emits a photon, returning to its ground state. The enzyme has a secondary acyl-CoA ligase activity when acting on L-firefly luciferin.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00427
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047077
CAS Registry Number: 61970-00-1
UniProtKB/Swiss-Prot:

References

  1. Green, A.A., McElroy, W.D.
    Crystalline firefly luciferase.
    Biochim. Biophys. Acta 20: 170-176 (1956). [PMID: 13315363]
  2. White, E.H., McCapra, F., Field, G.F. and McElroy, W.D.
    The structure and synthesis of firefly luciferin.
    J. Am. Chem. Soc. 83: 2402-2403 (1961).
  3. Hopkins, T.A., Seliger, H.H., White, E.H. and Cass, M.W.
    The chemiluminescence of firefly luciferin. A model for the bioluminescent reaction and identification of the product excited state.
    J. Am. Chem. Soc. 89: 7148-7150 (1967). [PMID: 6064360]
  4. White, E.H., Rapaport, E., Hopkins, T.A. and Seliger, H.H.
    Chemi- and bioluminescence of firefly luciferin.
    J. Am. Chem. Soc. 91: 2178-2180 (1969). [PMID: 5784183]
  5. Koo, J. A., Schmidt, S. P., Schuster, G. B.
    Bioluminescence of the firefly: key steps in the formation of the electronically excited state for model systems.
    Proc. Natl. Acad. Sci. U.S.A. 75: 30-33 (1978). [PMID: 272645]
  6. de Wet, J. R., Wood, K. V., Helinski, D. R., DeLuca, M.
    Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli.
    Proc. Natl. Acad. Sci. U.S.A. 82: 7870-7873 (1985). [PMID: 3906652]
  7. Nakamura, M., Maki, S., Amano, Y., Ohkita, Y., Niwa, K., Hirano, T., Ohmiya, Y., Niwa, H.
    Firefly luciferase exhibits bimodal action depending on the luciferin chirality.
    Biochem. Biophys. Res. Commun. 331: 471-475 (2005). [PMID: 15850783]
  8. Sundlov, J. A., Fontaine, D. M., Southworth, T. L., Branchini, B. R., Gulick, A. M.
    Crystal structure of firefly luciferase in a second catalytic conformation supports a domain alternation mechanism.
    Biochemistry 51: 6493-6495 (2012). [PMID: 22852753]

[EC 1.13.12.7 created 1976, modified 1981, modified 1982, modified 2017]