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EC 1.13.12.7 Details
show Brenda entryEC number
1.13.12.7
Accepted name
firefly luciferase
Reaction
D-firefly luciferin + O2 + ATP = firefly oxyluciferin + CO2 + AMP + diphosphate + hν
Other name(s)
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)
Systematic name
D-firefly luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)
CAS registry number
61970-00-1
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
created 1976, modified 1981, modified 1982, modified 2017
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1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.13.12.10 created 1989, modified 1999, deleted 2001 1.13.99.2 created 1972, deleted 1992 1.13.99.4 created 1989, deleted 1992 1.13.99.5 created 1999, deleted 2001
