CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.300 | GMP Synthetase; Chain A, domain 3 |
|
3.30.300.30 | ANL, C-terminal domain |
Domain Context
CATH Clusters
| Superfamily | 3.30.300.30 |
| Functional Family | 4-coumarate--CoA ligase 2 |
Enzyme Information
| 1.13.12.7 |
Firefly luciferase.
based on mapping to UniProt P13129
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)
| P13129 |
LUCI_LUCCR
Luciola cruciata
Luciferin 4-monooxygenase
|
PDB Structure
| PDB | 2D1R |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural basis for the spectral difference in luciferase bioluminescence.
Nature
|
