CATH Classification
Level | CATH Code | Description |
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2 | Mainly Beta |
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2.30 | Roll |
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2.30.38 | Luciferase; domain 3 |
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2.30.38.10 | Luciferase; Domain 3 |
Domain Context
CATH Clusters
Superfamily | Luciferase; Domain 3 |
Functional Family | Luciferin 4-monooxygenase |
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.
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UniProtKB Entries (1)
P13129 |
LUCI_LUCCR
Luciola cruciata
Luciferin 4-monooxygenase
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PDB Structure
PDB | 2D1S |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Structural basis for the spectral difference in luciferase bioluminescence.
Nature
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