CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.980
Functional Family Luciferin 4-monooxygenase

Enzyme Information

1.13.12.7
Firefly luciferase.
based on mapping to UniProt P08659
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 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 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 emits a photon, returning to its ground state. -!- The enzyme has a secondary acyl-CoA ligase activity when acting on L-firefly luciferin.

UniProtKB Entries (1)

P08659
LUCI_PHOPY
Photinus pyralis
Luciferin 4-monooxygenase

PDB Structure

PDB 4G36
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of firefly luciferase in a second catalytic conformation supports a domain alternation mechanism.
Sundlov, J.A., Fontaine, D.M., Southworth, T.L., Branchini, B.R., Gulick, A.M.
Biochemistry