Information on EC 1.13.12.18 - dinoflagellate luciferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.12.18
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RECOMMENDED NAME
GeneOntology No.
dinoflagellate luciferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dinoflagellate luciferin + O2 = oxidized dinoflagellate luciferin + H2O + hnu
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
dinoflagellate-luciferin:oxygen 132-oxidoreductase
A luciferase from dinoflagelates such as Gonyaulax polyedra, Lingulodinium polyedrum, Noctiluca scintillans, and Pyrocystis lunula. It is a single protein with three luciferase domains. The luciferin is strongly bound by a luciferin binding protein above a pH of 7.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Gonyaulax polyedra
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Manually annotated by BRENDA team
formerly Gonyaulax polyedra
UniProt
Manually annotated by BRENDA team
no activity in Cachonina illdefina
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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in Lingulodinium polyedrum, three components are involved in luminescence: the enzyme luciferase, the substrate luciferin, and a luciferin-binding protein which protects luciferin from autoxidation
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dinoflagellate luciferin + O2
?
show the reaction diagram
dinoflagellate luciferin + O2
oxidized dinoflagellate luciferin + H2O + hv
show the reaction diagram
additional information
?
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each of the three domains of Lingulodinium polyedrum luciferase encodes an active luciferase that catalyzes the oxidation of a chlorophyll-derived open tetrapyrrole (dinoflagellate luciferin) to produce blue light
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dinoflagellate luciferin + O2
?
show the reaction diagram
dinoflagellate luciferin + O2
oxidized dinoflagellate luciferin + H2O + hv
show the reaction diagram
additional information
?
-
O77206
each of the three domains of Lingulodinium polyedrum luciferase encodes an active luciferase that catalyzes the oxidation of a chlorophyll-derived open tetrapyrrole (dinoflagellate luciferin) to produce blue light
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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luciferase is not a Mn2+, Mg2+ , or Ca2+ metalloprotein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chlorotetracycline
cyanide
Sodium azide
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025
dinoflagellate luciferin
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in 0.2 M sodium phosphate, 0.25 mM EDTA, 0.1 mg/ml of bovine serum albumin at pH 6.3, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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the optimum pH of Lingulodinium polyedrum luciferase and for each of its domains is approximately 6.0
6.5
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Lingulodinium polyedrum luciferase domain 3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
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isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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SDS-PAGE
75000
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GST-LCF fusion protein, SDS-PAGE
100000
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about 100000 Da, native protein, SDS-PAGE
130000
gel filtration
137000
161000
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full-length enzyme, SDS-PAGE
420000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
domains D2-LCF and D3-LCF, sitting drop vapor diffusion method, using 13% (w/v) PEG 10000, 0.075 M bicine pH 7.7, 25% (v/v) glycerol for domain D2-LCF and 18-20% methyl ether PEG 2000, 100 mM EPPS buffer pH 7.8-8.4 for domain D3-LCF
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Lingulodinium polyedrum luciferase domain 3, vapor diffusion method, using 18-20% (w/v) polyethylene glycol 2000 methyl ether and 100 mM (2-hydroxyethyl)piperazine-N-(3-propanesulfonic acid) (pH 8.0)
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7 - 8
7.5
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LCF is inactive at pH 7.5
712941
8
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the activity of the full-length native enzyme drops to near zero at pH 8.0, the activity of domain fragments also peaks at pH 6.3 but remains high at 8.0
711192
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation
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ammonium sulfate precipitation and DEAE-Bio-Gel A column chromatography
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ammonium sulfate precipitation, Chelex column chromatography, hydroxylapatite column chromatography, and Ultrogel gel filtration
DEAE column chromatography
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domain D2-LCF and D3-LCF
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glutathione-Sepharose column chromatography
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Ni-NTA column chromatography
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Ni-NTA resin column chromatography
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nickel metal chelate column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
deletion mutants for N- or C-terminal regions of domain 3 of the luciferase are expressed in Escherichia coli BL21(DE3) cells
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domains D2-LCF and D3-LCF are expressed in Escherichia coli
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expressed in Escherichia coli JM 109 cells
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expressed in Escherichia coli strain M15 and in Sf21 insect cells
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expressed in Escherichia coli XLl-blue cells
expressed in NIH-3T3, A-549, and COS-7 cells
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histidine-tagged Lingulodinium polyedrum luciferase domain 3 is expressed in Escherichia coli BL21(DE3) cells
the three intramolecularly homologous domains are separately cloned and expressed in Escherichia coli JM109 cells as fusion proteins
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
dinoflagellate luciferase activity is highest during the early night phase
luciferase activity in cell-free extracts of Gonyaulax polyedm undergoes a cyclic daily change such that activities of extracts made in the middle of the night phase may be 10 times greater than in extracts of day phase cells. The circadian rhythm of luciferase activity is a result of biological clock-controlled synthesis and/or degradation of the luciferase polypeptide
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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the dinoflagellate luciferase gene is an efficient marker of gene expression in mammalian cells