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Information on EC 1.13.12.7 - firefly luciferase and Organism(s) Luciola cruciata and UniProt Accession P13129

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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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This record set is specific for:
Luciola cruciata
UNIPROT: P13129
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The taxonomic range for the selected organisms is: Luciola cruciata
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, firefly luciferin luciferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
firefly luciferase
-
firefly luciferase
-
-
-
-
firefly luciferin luciferase
-
-
-
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luciferase (firefly luciferin)
-
-
-
-
Photinus luciferin 4-monooxygenase (ATP-hydrolyzing)
-
-
-
-
Photinus pyralis luciferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-luciferin + ATP + O2
luciferyl-adenylate + diphosphate
show the reaction diagram
-
-
-
r
decanoic acid + ATP + CoA
decanoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
?
dehydroluciferin + ATP
dehydroluciferyl-AMP + diphosphate
show the reaction diagram
-
-
-
r
lauric acid + ATP + CoA
lauroyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
?
luciferyl-adenylate + O2
oxyluciferin + AMP + CO2 + hv
show the reaction diagram
-
-
-
ir
myristic acid + ATP + CoA
myristoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
?
R-COOH + ATP
R-CO-AMP + diphosphate
show the reaction diagram
-
-
-
r
arachidonic acid + ATP + CoA
arachidonoyl-CoA + ?
show the reaction diagram
-
-
-
-
?
linoleic acid + ATP + CoA
linoleoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
linolenic acid + ATP + CoA
linolenoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
oleic acid + ATP + CoA
oleoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
no fatty acyl-CoA synthetase activity with octanoic acid and palmitic acid
-
-
?
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
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
essential
Mg2+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dehydroluciferin
-
dehydroluciferyl adenylate
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oxyluciferin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
essential for luminescence reaction
molecular oxygen
essential for luminescence reaction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0024 - 0.0047
D-luciferin
0.0163
lauric acid
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.651
lauric acid
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
dehydroluciferyl adenylate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
fatty acyl-CoA synthesis, acyl-adenylate/thioester-forming enzyme
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LUCI_LUCCR
548
0
60017
Swiss-Prot
other Location (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S286N
red bioluminescence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
a chimeric protein derived from Photinus pyralis and Luciola cruciata luciferases is more stable than the wild type enzyme, retaining 75% of the activity after 10 min at 50°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, gel filtration, hydroxyapatite HPLC
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a chimeric protein derived from Photinus pyralis and Luciola cruciata luciferases expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirokawa, K.; Kajiyama, N.; Murakami, S.
Improved practical usefulness of firefly luciferase by gene chimerization and random mutagenesis
Biochim. Biophys. Acta
1597
271-279
2002
Luciola cruciata, Photinus pyralis
Manually annotated by BRENDA team
Oba, Y.; Sato, M.; Ojika, M.; Inouye, S.
Enzymatic and genetic characterization of firefly luciferase and Drosophila CG6178 as a fatty acyl-CoA synthetase
Biosci. Biotechnol. Biochem.
69
819-828
2005
Photinus pyralis (P08659), Luciola cruciata (P13129)
Manually annotated by BRENDA team
Oba, Y.; Ojika, M.; Inouye, S.
Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase
FEBS Lett.
540
251-254
2003
Luciola cruciata, Photinus pyralis
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