Information on EC 1.13.12.18 -

Information on EC 1.13.12.18 - dinoflagellate luciferase:

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EC NUMBER	COMMENTARY
1.13.12.18	-

RECOMMENDED NAME	GeneOntology No.
dinoflagellate luciferase	-

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
dinoflagellate luciferin + O2 = oxidized dinoflagellate luciferin + H2O + hnu		-	-	-	-

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

PATHWAY	KEGG Link	MetaCyc Link
No entries in this field

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.

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
D2-LCF	Lingulodinium polyedrum	-	second luciferase domain	710709
D3-LCF	Lingulodinium polyedrum	-	third luciferase domain	710709
LCF	Lingulodinium polyedrum	-	-	711276, 712940, 712941, 713390

CAS REGISTRY NUMBER	COMMENTARY
No entries in this field

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Lingulodinium polyedrum	-	713391	O77206	UniProt
Lingulodinium polyedrum	formerly Gonyaulax polyedra	710709, 710987, 711192, 712331, 712332, 712539, 712940, 712941, 713390	-	-
Lingulodinium polyedrum	formerly Gonyaulax polyedra	711276	O77206	UniProt
Lingulodinium polyedrum	formerly known as Gonyaulax polyedra	713206	-	-
Lingulodinium polyedrum 70	formerly Gonyaulax polyedra	712331	-	-
Lingulodinium polyedrum GP70	formerly Gonyaulax polyedra	711276	O77206	UniProt
no activity in Cachonina illdefina	-	712544	-	-
Noctiluca miliaris	-	712544	-	-
Noctiluca scintillans	-	713393	-	-
Pyrocystis fusiformis	-	710987, 712544	-	-
Pyrocystis lunula	-	710987, 712101	-	-
Pyrocystis noctiluca	-	712544	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
physiological function	Lingulodinium polyedrum	-	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	712332

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
(1S,2S,3S)-1-carboxy-3-(2-carboxyethyl)-12-ethyl-2,8,13,18-tetramethyl-17-vinyl-1,2,3,21-tetrahydro-5,7-ethanobilene-a-19(16H),52-dione + O2	?		Lingulodinium polyedrum	-	-	712539, 713206	-	-	?
dinoflagellate luciferin + O2	oxidized dinoflagellate luciferin + H2O + hv		Pyrocystis lunula	-	-	710987, 712101	-	-	?
dinoflagellate luciferin + O2	oxidized dinoflagellate luciferin + H2O + hv		Lingulodinium polyedrum	-	-	710709, 710987, 711192, 712331, 712539, 712940, 713206, 713390	-	-	?
dinoflagellate luciferin + O2	oxidized dinoflagellate luciferin + H2O + hv		Lingulodinium polyedrum	-	-	712332, 712941	-	-	ir
dinoflagellate luciferin + O2	oxidized dinoflagellate luciferin + H2O + hv		Lingulodinium polyedrum	O77206	-	711276, 713391	-	-	?
dinoflagellate luciferin + O2	oxidized dinoflagellate luciferin + H2O + hv		Pyrocystis fusiformis	-	-	710987, 712544	-	-	?
dinoflagellate luciferin + O2	oxidized dinoflagellate luciferin + H2O + hv		Pyrocystis noctiluca, Noctiluca miliaris	-	-	712544	-	-	?
dinoflagellate luciferin + O2	oxidized dinoflagellate luciferin + H2O + hv		Noctiluca scintillans	-	-	713393	-	-	?
additional information	?	-	Lingulodinium polyedrum	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	713391	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
(1S,2S,3S)-1-carboxy-3-(2-carboxyethyl)-12-ethyl-2,8,13,18-tetramethyl-17-vinyl-1,2,3,21-tetrahydro-5,7-ethanobilene-a-19(16H),52-dione + O2	?		Lingulodinium polyedrum	-	-	712539, 713206	-	-
dinoflagellate luciferin + O2	oxidized dinoflagellate luciferin + H2O + hv		Lingulodinium polyedrum	-	-	710709, 713390	-	-
dinoflagellate luciferin + O2	oxidized dinoflagellate luciferin + H2O + hv		Lingulodinium polyedrum	O77206	-	711276	-	-
additional information	?	-	Lingulodinium polyedrum	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	713391	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Ca2+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	increases the flash height and the total light emitted by dinoflagellate luciferase	710987
Mg2+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	increases the flash height and the total light emitted by dinoflagellate luciferase	710987
Mn2+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	increases the flash height and the total light emitted by dinoflagellate luciferase	710987
additional information	Lingulodinium polyedrum	-	luciferase is not a Mn2+, Mg2+ , or Ca2+ metalloprotein	712331

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
Ag+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	-	710987	2D-image
chlorotetracycline	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	-	710987	2D-image
Co2+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	-	710987	2D-image
Cu2+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	inhibits the light emission by dinoflagellate luciferase	710987	2D-image
cyanide	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	-	710987	2D-image
EDTA	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	-	710987	2D-image
EGTA	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	-	710987	2D-image
Fe2+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	inhibits the light emission by dinoflagellate luciferase	710987	2D-image
Fe3+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	inhibits the light emission by dinoflagellate luciferase	710987	2D-image
Ni2+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	inhibits the light emission by dinoflagellate luciferase	710987	2D-image
Pb2+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	-	710987	2D-image
Sodium azide	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	-	710987	2D-image
Sr2+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	-	710987	2D-image
Zn2+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	inhibits the light emission by dinoflagellate luciferase	710987	2D-image
Hg2+	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	-	710987	2D-image
additional information	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	after a 15 min incubation at pH 8.0 and 20�C with subtilisin, trypsin, chymotrypsin, pepsin, carboxypeptidase, and leucine aminopeptidase, the flash height measured in the presence of saturating luciferin is 50% lowered and, after 1 h, the flash height is 10% of the control. Moreover, proteolysis of the extracts completely inactivates the luciferase	710987	-

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.0025	-	dinoflagellate luciferin	Lingulodinium polyedrum	-	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	712331	2D-image

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
additional information	-	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	the crude extract has a specific activity of 0.000000258 at pH 8.0 and 20�C and the purified enzyme shows a specific activity of 0.00000348 quanta/min/mg at pH 8.0 and 20�C	710987

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
5.5	-	Pyrocystis lunula	-	-	712101
6	-	Lingulodinium polyedrum	-	the optimum pH of Lingulodinium polyedrum luciferase and for each of its domains is approximately 6.0	713206
6.3	-	Lingulodinium polyedrum	-	full-length native enzyme	711192
6.3	-	Lingulodinium polyedrum	-	-	712941
6.5	-	Lingulodinium polyedrum	-	Lingulodinium polyedrum luciferase domain 3	713206
7	-	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	-	710987

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
20	-	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	about 20�C	710987

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
5.4	-	Lingulodinium polyedrum	-	isoelectric focusing	710987
5.7	-	Pyrocystis fusiformis, Pyrocystis lunula	-	isoelectric focusing	710987

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
No entries in this field

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
cytoplasm	Lingulodinium polyedrum	-	cytoplasmic dense bodies with a finely vermiculate texture	5737	712539
mucocyst	Noctiluca miliaris, Pyrocystis fusiformis, Pyrocystis noctiluca	-	-	36000	712544
scintillon	Lingulodinium polyedrum	-	-	36007	710709, 712539, 712940, 712941
trichocyst	Lingulodinium polyedrum	-	the space between the crystalline shaft and the sheaths of mature trichocysts	55039	712539
vesicle	Noctiluca miliaris, Pyrocystis fusiformis, Pyrocystis noctiluca	-	dense vesicles in the peripheral cytoplasm	31982	712544

PDB	SCOP	CATH	ORGANISM
No entries in this field

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
30000	-	Lingulodinium polyedrum	-	SDS-PAGE	710987
40000	-	Pyrocystis fusiformis, Pyrocystis lunula	-	SDS-PAGE	710987
75000	-	Lingulodinium polyedrum	-	GST-LCF fusion protein, SDS-PAGE	712940
100000	-	Noctiluca scintillans	-	about 100000 Da, native protein, SDS-PAGE	713393
130000	-	Lingulodinium polyedrum	O77206	gel filtration	711276
137000	-	Lingulodinium polyedrum	-	calculated from amino acid sequence	710709
137000	-	Lingulodinium polyedrum	-	full-length enzyme, calculated from amino acid sequence	712940
161000	-	Lingulodinium polyedrum	-	full-length enzyme, SDS-PAGE	712940
420000	-	Lingulodinium polyedrum	-	gel filtration	712331

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
?	Lingulodinium polyedrum	-	x * 30000, SDS-PAGE	710987
?	Pyrocystis fusiformis, Pyrocystis lunula	-	x * 40000, SDS-PAGE	710987
homotrimer	Lingulodinium polyedrum	-	2 * 44000, SDS-PAGE	710709
homotrimer	Lingulodinium polyedrum	-	3 * 130000, SDS-PAGE	712331
homotrimer	Lingulodinium polyedrum	-	2 * 42000, SDS-PAGE	713206

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	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	Lingulodinium polyedrum	-	710709
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)	Lingulodinium polyedrum	O77206	713391

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6.7	8	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	the crude enzyme extracts are more stable at pH 8.0 and 5�C in HEPES buffer than at pH 6.7 and 5�C	710987
7.5	-	Lingulodinium polyedrum	-	LCF is inactive at pH 7.5	712941
8	-	Lingulodinium polyedrum	-	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	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
20	40	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	-	at 20�C the luciferase is progressively inactivated after a 4 h incubation time at each pH, about 50% residual activity is observed at 30�C, the enzyme appears completely inactive at 40�C and pH 7.9 and shows about 10% residual activity at 40�C and pH 6.7	710987

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
guanidine-HCl	Lingulodinium polyedrum	-	at 18 and 5�C guanidine-HCl in the concentration range from 2-6 M, denatures irreversibly the luciferase. Luciferin does not protect the luciferase against denaturation by this agent	710987
guanidine-HCl	Pyrocystis fusiformis	-	at 18�C and 5�C guanidine-HCl in the concentration range from 2-6 M, denatures irreversibly the luciferase. Luciferin does not protect the luciferase against denaturation by this agent	710987
guanidine-HCl	Pyrocystis lunula	-	at 18 and 5�C guanidine-HCl in the concentration range from 2-6 M, denatures irreversibly the luciferase. Luciferin does not protect the luciferase against denaturation by this agent	710987
urea	Lingulodinium polyedrum	-	at 18 and 5�C urea in the concentration range from 2-8 M, denatures irreversibly the luciferase. Luciferin does not protect the luciferase against denaturation by this agent	710987
urea	Pyrocystis fusiformis	-	at 18�C and 5�C urea in the concentration range from 2-8 M, denatures irreversibly the luciferase. Luciferin does not protect the luciferase against denaturation by this agent	710987
urea	Pyrocystis lunula	-	at 18 and 5�C urea in the concentration range from 2-8 M, denatures irreversibly the luciferase. Luciferin does not protect the luciferase against denaturation by this agent	710987

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
ammonium sulfate precipitation	Lingulodinium polyedrum	-	712331
ammonium sulfate precipitation and DEAE-Bio-Gel A column chromatography	Lingulodinium polyedrum	-	712332
ammonium sulfate precipitation, Chelex column chromatography, hydroxylapatite column chromatography, and Ultrogel gel filtration	Lingulodinium polyedrum	-	710987
DEAE column chromatography	Lingulodinium polyedrum	-	712941
domain D2-LCF and D3-LCF	Lingulodinium polyedrum	-	710709
glutathione-Sepharose column chromatography	Lingulodinium polyedrum	-	711192, 712940
Ni-NTA column chromatography	Lingulodinium polyedrum	-	713206
nickel metal chelate column chromatography	Lingulodinium polyedrum	O77206	713391
Ni-NTA resin column chromatography	Noctiluca scintillans	-	713393
ammonium sulfate precipitation, Chelex column chromatography, hydroxylapatite column chromatography, and Ultrogel gel filtration	Pyrocystis fusiformis, Pyrocystis lunula	-	710987

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
deletion mutants for N- or C-terminal regions of domain 3 of the luciferase are expressed in Escherichia coli BL21(DE3) cells	Lingulodinium polyedrum	-	713206
domains D2-LCF and D3-LCF are expressed in Escherichia coli	Lingulodinium polyedrum	-	710709
expressed in Escherichia coli JM 109 cells	Lingulodinium polyedrum	-	712940
expressed in Escherichia coli XLl-blue cells	Lingulodinium polyedrum	O77206	711276
histidine-tagged Lingulodinium polyedrum luciferase domain 3 is expressed in Escherichia coli BL21(DE3) cells	Lingulodinium polyedrum	O77206	713391
the three intramolecularly homologous domains are separately cloned and expressed in Escherichia coli JM109 cells as fusion proteins	Lingulodinium polyedrum	-	711192
expressed in Escherichia coli strain M15 and in Sf21 insect cells	Noctiluca scintillans	-	713393
expressed in NIH-3T3, A-549, and COS-7 cells	Pyrocystis lunula	-	712101

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
dinoflagellate luciferase activity is highest during the early night phase	Lingulodinium polyedrum	O77206	711276
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	Lingulodinium polyedrum	-	712331

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
additional information	Lingulodinium polyedrum	-	for each luciferase domain (D1, D2, D3) the removal of approximately 50 N-terminal amino acids results in an increase in the ratio of luciferase activity at pH 8.0 relative to that at pH 6.3. At pH 8.0, peptides D1167-486, D2535-897, and D3927-1241, lacking the first 55, 47, and 62 amino acids of their N-termini retain about 40%, 50%, and 70% of the pH 6.3 luciferase activity, respectively	711192
additional information	Lingulodinium polyedrum	-	deletion mutants for N-terminal region of domain 3 of the luciferase show above 20% of wild type activity, the activities of C-terminal deleted mutants decrease drastically to below 1% of wild type	713206

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
biotechnology	Pyrocystis lunula	-	the dinoflagellate luciferase gene is an efficient marker of gene expression in mammalian cells	712101

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
710709	Liu, L.; Im, H.; Cegielski, M.; LeMagueres, P.; Schultz, L.W.; Krause, K.L.; Hastings, J.W.	Characterization and crystallization of active domains of a novel luciferase from a marine dinoflagellate	Acta Crystallogr. Sect. D	59	761-764	2003	Lingulodinium polyedrum	PubMed
710987	Lecuyer, B.; Arrio, B.; Fresneau, C.; Volfin, P.	Dinoflagellate luciferases: purification of luciferases from Gonyaulax polyedra, Pyrocystis lunula, and Pyrocystis fusiformis	Arch. Biochem. Biophys.	196	371-384	1979	Lingulodinium polyedrum, Pyrocystis fusiformis, Pyrocystis lunula	PubMed
711192	Li, L.; Liu, L.; Hong, R.; Robertson, D.; Hastings, J.W.	N-terminal intramolecularly conserved histidines of three domains in Gonyaulax luciferase are responsible for loss of activity in the alkaline region	Biochemistry	40	1844-1849	2001	Lingulodinium polyedrum	PubMed
711276	Bae, Y.M.; Hastings, J.W.	Cloning, sequencing and expression of dinoflagellate luciferase DNA from a marine alga, Gonyaulax polyedra	Biochim. Biophys. Acta	1219	449-456	1994	Lingulodinium polyedrum	PubMed
712101	Suzuki, C.; Nakajima, Y.; Akimoto, H.; Wu, C.; Ohmiya, Y.	A new additional reporter enzyme, dinoflagellate luciferase, for monitoring of gene expression in mammalian cells	Gene	344	61-66	2005	Pyrocystis lunula	PubMed
712331	Dunlap, J.C.; Hastings, J.W.	The biological clock in Gonyaulax controls luciferase activity by regulating turnover	J. Biol. Chem.	256	10509-10518	1981	Lingulodinium polyedrum	PubMed
712332	Morse, D.; Pappenheimer, A.M., Jr.; Hastings, J.W.	Role of a luciferin-binding protein in the circadian bioluminescent reaction of Gonyaulax polyedra	J. Biol. Chem.	264	11822-11826	1989	Lingulodinium polyedrum	PubMed
712539	Nicolas, M.T.; Nicolas, G.; Johnson, C.H.; Bassot, J.M.; Hastings, J.W.	Characterization of the bioluminescent organelles in Gonyaulax polyedra (dinoflagellates) after fast-freeze fixation and antiluciferase immunogold staining	J. Cell Biol.	105	723-735	1987	Lingulodinium polyedrum	PubMed
712544	Nicolas, M.T.; Sweeney, B.M.; Hastings, J.W.	The ultrastructural localization of luciferase in three bioluminescent dinoflagellates, two species of Pyrocystis, and Noctiluca, using anti-luciferase and immunogold labelling	J. Cell Sci.	87	189-196	1987	no activity in Cachonina illdefina, Noctiluca miliaris, Pyrocystis fusiformis, Pyrocystis noctiluca	PubMed
712940	Li, L.	Gonyaulax luciferase: gene structure, protein expression, and purification from recombinant sources	Methods Enzymol.	305	249-258	2000	Lingulodinium polyedrum	PubMed
712941	Morse, D.; Mittag, M.	Dinoflagellate luciferin-binding protein	Methods Enzymol.	305	258-276	2000	Lingulodinium polyedrum	PubMed
713206	Suzuki-Ogoh, C.; Wu, C.; Ohmiya, Y.	C-terminal region of the active domain enhances enzymatic activity in dinoflagellate luciferase	Photochem. Photobiol. Sci.	7	208-211	2008	Lingulodinium polyedrum	PubMed
713390	Liu, L.; Wilson, T.; Hastings, J.W.	Molecular evolution of dinoflagellate luciferases, enzymes with three catalytic domains in a single polypeptide	Proc. Natl. Acad. Sci. USA	101	16555-16560	2004	Lingulodinium polyedrum	PubMed
713391	Schultz, L.W.; Liu, L.; Cegielski, M.; Hastings, J.W.	Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole	Proc. Natl. Acad. Sci. USA	102	1378-1383	2005	Lingulodinium polyedrum	PubMed
713393	Liu, L.; Hastings, J.W.	Two different domains of the luciferase gene in the heterotrophic dinoflagellate Noctiluca scintillans occur as two separate genes in photosynthetic species	Proc. Natl. Acad. Sci. USA	104	696-701	2007	Noctiluca scintillans	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 1.13.12.18)

NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM

IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)