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Information on EC 1.13.12.7 - firefly luciferase and Organism(s) Aquatica lateralis and UniProt Accession Q01158

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IUBMB Comments
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 CO2 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 (see EC 6.2.1.52).
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Aquatica lateralis
UNIPROT: Q01158
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The taxonomic range for the selected organisms is: Aquatica lateralis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
firefly luciferase, luciferin, photinus pyralis luciferase, beetle luciferase, pc3-luc, pplase, cbrluc, luciola italica luciferase, lucppy, oxygen 4-oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
firefly luciferase
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firefly luciferin luciferase
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luciferase (firefly luciferin)
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Photinus luciferin 4-monooxygenase (ATP-hydrolyzing)
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Photinus pyralis luciferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
D-firefly luciferin:oxygen 4-oxidoreductase (decarboxylating, ATP-hydrolysing)
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 CO2 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 (see EC 6.2.1.52).
CAS REGISTRY NUMBER
COMMENTARY hide
61970-00-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
show the reaction diagram
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
show the reaction diagram
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LUCI_AQULA
548
0
60125
Swiss-Prot
other Location (Reliability: 1)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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10 min at 50°C decreases activity by 90%
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, gel filtration, hydroxyapatite HPLC
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the wild type and three mutants in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
firefly luciferase is widely used in molecular biology and bioanalytical systems as a reporter molecule due to the high quantum yield of the bioluminescence, availability of stable mutant forms of the enzyme with prescribed spectral characteristics and abundance of bacterial expression systems suitable for production of recombinant proteins in limitless quantities. Fusion proteins of luciferase are described with biotin-binding domain and treptavidin, with proteins A and G, antibodies, with DNA- and RNA-binding proteins, as well as fusion proteins designed for BRET systems. The firefly luciferase-based fusion proteins are represented as an effective tool for the development of different bioanalytical systems such as (1) systems in which luciferase is attached to the surface of the target and the bioluminescence signal is detected from the specific complexes formed, (2) BRET-based systems, in which the specific interaction induces changes in the bioluminescence spectrum, and (3) systems that use modified or split luciferases, in which the luciferase activity changes under the action of the analyte. All these systems have wide application in biochemical analysis of physiologically important compounds, for the detection of pathogenic bacteria and viruses, for evaluation of protein-protein interactions, assaying of metabolites involved in cell communication and cell signaling
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kajiyama, N.; Nakano, E.
Enhancement of thermostability of firefly luciferase from Luciola lateralis by a single amino acid substitution
Biosci. Biotechnol. Biochem.
58
1170-1171
1994
Aquatica lateralis
Manually annotated by BRENDA team
Inouye, S.
Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions
Cell. Mol. Life Sci.
67
387-404
2010
Pyrearinus termitilluminans (AF116843), Photinus pyralis (P08659), Luciola cruciata (P13129), Aquatica lateralis (Q01158), Lampyroidea maculata (Q1WLP6), Luciola parvula (Q25118), Pyrocoelia miyako (Q26076), Luciola mingrelica (Q26304), Lampyris noctiluca (Q27688), Photuris pensylvanica (Q27757), Lampyris turkestanicus (Q5UFR2), Cratomorphus distinctus (Q5USC8), Pyrophorus mellifluus (Q717B6), Pyrophorus plagiophthalamus (Q718F0), Hotaria unmunsana (Q8T6U3), Pyrocoelia rufa (Q9GPF9), Phrixothrix hirtus (Q9U4U7), Phrixothrix vivianii (Q9U4U8)
Manually annotated by BRENDA team
Smirnova, D.V.; Ugarova, N.N.
Firefly luciferase-based fusion proteins and their applications in bioanalysis
Photochem. Photobiol.
93
436-447
2017
Photinus pyralis (P08659), Aquatica lateralis (Q01158), Luciola mingrelica (Q26304)
Manually annotated by BRENDA team