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ENZYME

ENZYME entry: EC 1.13.12.7

PURL: https://purl.expasy.org/enzyme/EC/1.13.12.7
Accepted Name
firefly luciferase
Alternative Name(s)
luciferase
Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing)
Photinus pyralis luciferase
Reaction catalysed
firefly D-luciferin + ATP + O2 = firefly oxyluciferin + hnu + AMP + CO2 + diphosphate
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 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.
Cross-references
BRENDA1.13.12.7
EC2PDB1.13.12.7
ExplorEnz1.13.12.7
KEGG Ligand Database for Enzyme Nomenclature1.13.12.7
IUBMB Enzyme Nomenclature1.13.12.7
MEDLINEFind literature relating to 1.13.12.7
MetaCyc1.13.12.7
Rhea expert-curated reactions1.13.12.7
UniProtKB/Swiss-Prot
Q01158, LUCI_AQULAQ26304, LUCI_LUCMIP13129, LUCI_NIPCR
Q27757, LUCI_PHOPEP08659, LUCI_PHOPY

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