To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
ENZYME entry: EC 18.104.22.168
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||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
, with possibility to download in different formats, align etc.
entries corresponding to 1.13.12.-
entries corresponding to 1.13.-.-
entries corresponding to 1.-.-.-