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ENZYME entry: EC 1.13.12.7

Accepted Name
Firefly luciferase.
Alternative Name(s)
Luciferase.
Photinus pyralis luciferase.
Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing).
Reaction catalysed
D-firefly luciferin + O(2) + ATP <=> firefly oxyluciferin + CO(2) + AMP + diphosphate + light
Comment(s)
  • 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 CO(2) 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.
Cross-references
PROSITEPDOC00427
BRENDA1.13.12.7
EC2PDB1.13.12.7
ExplorEnz1.13.12.7
PRIAM enzyme-specific profiles1.13.12.7
KEGG Ligand Database for Enzyme Nomenclature1.13.12.7
IUBMB Enzyme Nomenclature1.13.12.7
IntEnz1.13.12.7
MEDLINEFind literature relating to 1.13.12.7
MetaCyc1.13.12.7
Rhea expert-curated reactions1.13.12.7
UniProtKB/Swiss-Prot
Q01158, LUCI_AQULA;  P13129, LUCI_LUCCR;  Q26304, LUCI_LUCMI;  
Q27757, LUCI_PHOPE;  P08659, LUCI_PHOPY;  

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