ENZYME entry: EC 1.13.12.7
Accepted Name |
firefly luciferase.
|
Alternative Name(s) |
luciferase. |
Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing). |
Photinus pyralis luciferase. |
Reaction catalysed |
ATP + firefly D-luciferin + O2 <=> AMP + CO2 + diphosphate + firefly oxyluciferin + hnu |
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 |
BRENDA | 1.13.12.7 |
EC2PDB | 1.13.12.7 |
ExplorEnz | 1.13.12.7 |
PRIAM enzyme-specific profiles | 1.13.12.7 |
KEGG Ligand Database for Enzyme Nomenclature | 1.13.12.7 |
IUBMB Enzyme Nomenclature | 1.13.12.7 |
IntEnz | 1.13.12.7 |
MEDLINE | Find literature relating to 1.13.12.7 |
MetaCyc | 1.13.12.7 |
Rhea expert-curated reactions | 1.13.12.7 |
UniProtKB/Swiss-Prot |
|
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