KEGG   ENZYME: 1.13.12.7Help
Entry
EC 1.13.12.7                Enzyme                                 

Name
firefly luciferase;
Photinus-luciferin 4-monooxygenase (ATP-hydrolysing);
luciferase (firefly luciferin);
Photinus luciferin 4-monooxygenase (adenosine triphosphate-hydrolyzing);
firefly luciferin luciferase;
Photinus pyralis luciferase;
Photinus-luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)
BRITE hierarchy
Sysname
D-firefly luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)
Reaction(IUBMB)
D-firefly luciferin + O2 + ATP = firefly oxyluciferin + CO2 + AMP + diphosphate + hnu [RN:R04036]
Reaction(KEGG)
Substrate
D-firefly luciferin [CPD:C02740];
O2 [CPD:C00007];
ATP [CPD:C00002]
Product
firefly oxyluciferin [CPD:C03797];
CO2 [CPD:C00011];
AMP [CPD:C00020];
diphosphate [CPD:C00013];
hnu [CPD:C00205]
Comment
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 (see EC 6.2.1.52).
History
EC 1.13.12.7 created 1976, modified 1981, modified 1982, modified 2017
Orthology
K05914  photinus-luciferin 4-monooxygenase (ATP-hydrolysing)
Reference
1  [PMID:13315363]
  Authors
GREEN AA, MCELROY WD
  Title
Crystalline firefly luciferase.
  Journal
Biochim Biophys Acta 20:170-6 (1956)
DOI:10.1016/0006-3002(56)90275-X
Reference
2
  Authors
White, E.H., McCapra, F., Field, G.F. and McElroy, W.D.
  Title
The structure and synthesis of firefly luciferin.
  Journal
J Am Chem Soc 83:2402-2403 (1961)
Reference
3  [PMID:6064360]
  Authors
Hopkins TA, Seliger HH, White EH, Cass MH.
  Title
The chemiluminescence of firefly luciferin. A model for the bioluminescent reaction and identification of the product excited state.
  Journal
J Am Chem Soc 89:7148-50 (1967)
Reference
4  [PMID:5784183]
  Authors
White EH, Rapaport E, Hopkins TA, Seliger HH.
  Title
Chemi- and bioluminescence of firefly luciferin.
  Journal
J Am Chem Soc 91:2178-80 (1969)
Reference
5  [PMID:272645]
  Authors
Koo JA, Schmidt SP, Schuster GB
  Title
Bioluminescence of the firefly: key steps in the formation of the electronically  excited state for model systems.
  Journal
Proc Natl Acad Sci U S A 75:30-3 (1978)
DOI:10.1073/pnas.75.1.30
Reference
6  [PMID:3906652]
  Authors
de Wet JR, Wood KV, Helinski DR, DeLuca M
  Title
Cloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli.
  Journal
Proc Natl Acad Sci U S A 82:7870-3 (1985)
DOI:10.1073/pnas.82.23.7870
Reference
7  [PMID:15850783]
  Authors
Nakamura M, Maki S, Amano Y, Ohkita Y, Niwa K, Hirano T, Ohmiya Y, Niwa H
  Title
Firefly luciferase exhibits bimodal action depending on the luciferin chirality.
  Journal
Biochem Biophys Res Commun 331:471-5 (2005)
DOI:10.1016/j.bbrc.2005.03.202
Reference
8  [PMID:22852753]
  Authors
Sundlov JA, Fontaine DM, Southworth TL, Branchini BR, Gulick AM
  Title
Crystal structure of firefly luciferase in a second catalytic conformation supports a domain alternation mechanism.
  Journal
Biochemistry 51:6493-5 (2012)
DOI:10.1021/bi300934s
Other DBs
ExplorEnz - The Enzyme Database: 1.13.12.7
IUBMB Enzyme Nomenclature: 1.13.12.7
ExPASy - ENZYME nomenclature database: 1.13.12.7
BRENDA, the Enzyme Database: 1.13.12.7
CAS: 61970-00-1

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