CATH Classification

Domain Context

CATH Clusters

Superfamily N-terminal domain of ligase-like
Functional Family Long-chain-fatty-acid--CoA ligase FadD

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 3IES
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Molecular basis for the high-affinity binding and stabilization of firefly luciferase by PTC124.
Auld, D.S., Lovell, S., Thorne, N., Lea, W.A., Maloney, D.J., Shen, M., Rai, G., Battaile, K.P., Thomas, C.J., Simeonov, A., Hanzlik, R.P., Inglese, J.
Proc.Natl.Acad.Sci.USA