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Information on EC 1.13.12.7 - firefly luciferase and Organism(s) Luciola italica and UniProt Accession Q1AG35

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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 italica
UNIPROT: Q1AG35
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Word Map
The taxonomic range for the selected organisms is: Luciola italica
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, ppy re-ts, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Luciola italica luciferase
-
firefly luciferase
-
-
-
-
firefly luciferin luciferase
-
-
-
-
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-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
show the reaction diagram
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
assay at, mutants luc2 and PLG2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at, mutants luc2 and PLG2
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q1AG35_9COLE
548
0
60496
TrEMBL
other Location (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of the chimeric mutant luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase in HEK-293 cells and in Escherichia coli strain BL21(DE3)pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Branchini, B.R.; Southworth, T.L.; Fontaine, D.M.; Kohrt, D.; Talukder, M.; Michelini, E.; Cevenini, L.; Roda, A.; Grossel, M.J.
An enhanced chimeric firefly luciferase-inspired enzyme for ATP detection and bioluminescence reporter and imaging applications
Anal. Biochem.
484
148-153
2015
Photinus pyralis (P08659), Photinus pyralis, Luciola italica (Q1AG35), Luciola italica
Manually annotated by BRENDA team
Branchini, B.R.; Southworth, T.L.; Fontaine, D.M.; Davis, A.L.; Behney, C.E.; Murtiashaw, M.H.
A Photinus pyralis and Luciola italica chimeric firefly luciferase produces enhanced bioluminescence
Biochemistry
53
6287-6289
2014
Photinus pyralis (P08659), Photinus pyralis, Luciola italica (Q1AG35), Luciola italica
Manually annotated by BRENDA team