CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.12780 | N-terminal domain of ligase-like |
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 | 3IEP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Molecular basis for the high-affinity binding and stabilization of firefly luciferase by PTC124.
Proc.Natl.Acad.Sci.USA
|
