ENZYME entry: EC 22.214.171.124
View entry in original ENZYME format
View entry in raw text format (no links)
in this entry
|Photinus pyralis luciferase.|
|Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing).|
|D-firefly luciferin + O(2) + ATP <=> firefly oxyluciferin + CO(2) + AMP + diphosphate + light|
- 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
- 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 emitts a photon, returning to its ground
- The enzyme has a secondary acyl-CoA ligase activity when acting on
|PRIAM enzyme-specific profiles||126.96.36.199|
|KEGG Ligand Database for Enzyme Nomenclature||188.8.131.52|
|IUBMB Enzyme Nomenclature||184.108.40.206|
|MEDLINE||Find literature relating to 220.127.116.11|
, with possibility to download in different formats, align etc.
entries corresponding to 1.13.12.-
entries corresponding to 1.13.-.-
entries corresponding to 1.-.-.-