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Information on EC 1.13.12.5 - Renilla-type luciferase and Organism(s) Renilla reniformis and UniProt Accession P27652
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1.13.12.5 Renilla-type luciferaseIUBMB Comments
This enzyme has been studied from the soft coral Renilla reniformis. Before the reaction occurs the substrate is sequestered by a coelenterazine-binding protein. Elevation in the concentration of calcium ions releases the substrate, which then interacts with the luciferase. Upon binding the substrate, the enzyme catalyses an oxygenation, producing a very short-lived hydroperoxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO2 molecule. The spontaneous breakdown of the dioxetanone releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of the coelenteramide product, which is the singlet form of the monoanion. In vivo the product undergoes the process of nonradiative energy transfer to an accessory protein, a green fluorescent protein (GFP), which results in green bioluminescence. In vitro, in the absence of GFP, the product emits blue light.
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Word Map
- 1.13.12.5
-
bioluminescence
-
luminescence
-
photoproteins
- firefly
- agonist
- ventricular
-
contractile
-
tension
- ferret
-
emit
-
twitch
-
isometric
-
papillary
-
depolarization
-
ca2+-sensitive
-
microinjected
- myocardium
-
sarcoplasmic
- aequorea
- caffeine
-
ryanodine
- myofilaments
-
inotropic
-
jellyfish
-
calcium-sensitive
- luciferases
- victoria
-
excitation-contraction
-
fura-2
-
replicons
-
ca2+cyt
-
tetanic
-
light-emitting
- analysis
-
glow
- trabeculae
- insp3
- biotechnology
- photinus
-
signal-to-background
-
ca2+-regulated
-
ca2+-triggered
- barnacle
-
luminometer
-
luminescence-based
-
myoplasmic
-
ca2+-mobilizing
- molecular biology
- diagnostics
- pharmacology
-
isovolumic
-
charge-coupled
-
luciferase-based
- pyralis
-
photomultiplier
The taxonomic range for the selected organisms is: Renilla reniformis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
aequorin, renilla luciferase, gaussia luciferase, gaussia princeps luciferase, renilla reniformis luciferase, rluc8, clytin, oplophorus luciferase, bfp-aq, gaussia-luciferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Renilla luciferase
-
RLuc
-
aequorin
-
-
-
-
luciferase (Renilla luciferin)
-
-
-
-
Renilla luciferin 2-monooxygenase
-
-
-
-
Renilla-luciferin 2-monooxygenase
Renilla-type luciferase
-
-
-
-
Renilla-luciferin 2-monooxygenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coelenterazine h + O2 = excited coelenteramide h monoanion + CO2
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
coelenterazine h:oxygen 2-oxidoreductase (decarboxylating)
This enzyme has been studied from the soft coral Renilla reniformis. Before the reaction occurs the substrate is sequestered by a coelenterazine-binding protein. Elevation in the concentration of calcium ions releases the substrate, which then interacts with the luciferase. Upon binding the substrate, the enzyme catalyses an oxygenation, producing a very short-lived hydroperoxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO2 molecule. The spontaneous breakdown of the dioxetanone releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of the coelenteramide product, which is the singlet form of the monoanion. In vivo the product undergoes the process of nonradiative energy transfer to an accessory protein, a green fluorescent protein (GFP), which results in green bioluminescence. In vitro, in the absence of GFP, the product emits blue light.
CAS REGISTRY NUMBER
COMMENTARY
346421-46-3
Gaussia luciferase
61869-41-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-benzyl-8-benzyl-6-(2-fluorophenylethynyl)imidazo[1,2-a]pyrazin-3(7H)-one + O2
? + CO2 + hv
-
-
-
?
2-benzyl-8-benzyl-6-(3-fluorophenylethynyl)imidazo[1,2-a]pyrazin-3(7H)-one + O2
? + CO2 + hv
-
-
-
?
2-benzyl-8-benzyl-6-(3-hydroxyphenylethynyl)imidazo[1,2-a]pyrazin-3(7H)-one + O2
? + CO2 + hv
-
-
-
?
2-benzyl-8-benzyl-6-(3-methylphenylethynyl)imidazo[1,2-a]pyrazin-3(7H)-one + O2
? + CO2 + hv
-
-
-
?
2-benzyl-8-benzyl-6-(4-fluorophenylethynyl)imidazo[1,2-a]pyrazin-3(7H)-one + O2
? + CO2 + hv
-
-
-
?
2-benzyl-8-benzyl-6-(phenylethynyl)imidazo[1,2-a]pyrazin-3(7H)-one + O2
? + CO2 + hv
-
-
-
?
2-benzyl-8-benzyl-6-[(1-fluoroethyl)-1,2,3-triazol-4]imidazo[1,2-a]pyrazin-3(7H)-one + O2
? + CO2 + hv
-
-
-
?
2-benzyl-8-benzyl-6-[(1-hydroxyethyl)-1,2,3-triazol-4]imidazo[1,2-a]pyrazin-3(7H)-one + O2
? + CO2 + hv
-
-
-
?
2-benzyl-8-benzyl-6-[(1-hydroxypropyl)-1,2,3-triazol-4]imidazo[1,2-a]pyrazin-3(7H)-one + O2
? + CO2 + hv
-
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hv
-
-
-
?
coelenterazine-h + O2
coelenteramide h + CO2 + hv
substrate binding structure
-
-
?
12-benzyl-8-hydroxy-2-(4-hydroxybenzyl)-5,11-dihydrobenzo[f]imidazo[1,2-a]quinoxalin-3(6H)-one + O2
oxidized 12-benzyl-8-hydroxy-2-(4-hydroxybenzyl)-5,11-dihydrobenzo[f]imidazo[1,2-a]quinoxalin-3(6H)-one + CO2 + hnu
-
-
-
-
?
2,8-dibenzyl-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one + O2
oxidized 2,8-dibenzyl-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one + CO2 + hn
-
-
-
-
?
8-benzyl-2-(4-fluorobenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one + O2
oxidized 8-benzyl-2-(4-fluorobenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one + CO2 + hnu
-
-
-
-
?
8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one + O2
oxidized 8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one + CO2 + hn
-
-
-
-
?
benzylluciferin methyl ether + O2
oxidized benzylluciferin methyl ether + CO2 + hv
-
-
-
-
?
coelenterate-type luciferin + O2
oxidized coelenterate-type luciferin + CO2 + hv
-
-
-
-
?
coelenterazine h + O2
excited coelenteramide h monoanion + CO2
CAA01908.1
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
Renilla luciferin + O2
oxidized Renilla luciferin + CO2 + hv
-
-
-
-
?
coelenterazine h + O2
excited coelenteramide h monoanion + CO2
-
-
-
?
coelenterazine h + O2
excited coelenteramide h monoanion + CO2
an induced-fit mechanism is proposed where ligand-binding induces conformational changes of the active site. Insights regarding the controversial properties and the mechanism of the reaction catalysis of Renilla luciferase and its red-shifted light emittingvariant (Super RLuc 8)
-
-
?
3iso-coelenterazine + O2
?
-
relative activity to native coelenterazine: 11.6%
-
-
?
3iso-coelenterazine + O2
?
-
relative activity to native coelenterazine: 34.9%
-
-
?
3me-coelenterazine + O2
?
-
relative activity to native coelenterazine: 11.8%
-
-
?
3me-coelenterazine + O2
?
-
relative activity to native coelenterazine: 45.5%
-
-
?
3meo-coelenterazine + O2
?
-
relative activity to native coelenterazine: 5.5%
-
-
?
3meo-coelenterazine + O2
?
-
relative activity to native coelenterazine: 82.3%
-
-
?
alphameh-coelenterazine + O2
?
-
relative activity to native coelenterazine: 0.02%
-
-
?
alphameh-coelenterazine + O2
?
-
relative activity to native coelenterazine: 24.7%
-
-
?
cf3-coelenterazine + O2
?
-
relative activity to native coelenterazine: 16.8%
-
-
?
cf3-coelenterazine + O2
?
-
relative activity to native coelenterazine: 5%
-
-
?
et-coelenterazine + O2
?
-
relative activity to native coelenterazine: 1.2%
-
-
?
et-coelenterazine + O2
?
-
relative activity to native coelenterazine: 78.3%
-
-
?
h-coelenterazine + O2
?
-
relative activity to native coelenterazine: 12.4%
-
-
?
h-coelenterazine + O2
?
-
relative activity to native coelenterazine: 54.1%
-
-
?
i-coelenterazine + O2
?
-
relative activity to native coelenterazine: 0.3%
-
-
?
i-coelenterazine + O2
?
-
relative activity to native coelenterazine: 5.1%
-
-
?
me-coelenterazine + O2
?
-
relative activity to native coelenterazine: 5.2%
-
-
?
me-coelenterazine + O2
?
-
relative activity to native coelenterazine: 73.6%
-
-
?
meo-coelenterazine + O2
?
-
relative activity to native coelenterazine: 1.2%
-
-
?
meo-coelenterazine + O2
?
-
relative activity to native coelenterazine: 18.2%
-
-
?
additional information
?
-
design and synthesis of bioluminescent coelenterazine derivatives (alkynes and triazoles) with imidazopyrazinone C-6 extended substitution as substrates for Renilla luciferase, evaluation, substrate specificity, overview
-
-
?
additional information
?
-
dynamic light scattering has been used for the detection of protein-protein interaction between the IgG antibody and modified enzyme FcUni-RLuc, to which an Fc-binding peptide is bound and separated by a five-amino acid linker from RLuc. Analysis of FcUni-RLuc and Herceptin interaction
-
-
?
additional information
?
-
establishment and evaluation of an indirect autophagy flux assay based on monitoring the degradation of an autophagosome-associated fusion protein Rluc-LC3 by luminescence detection. The Rluc-LC3 assay is useful for the identification of genes, miRNAs, and small molecules that regulate autophagy flux in mammalian cells. LC3 is a subfamily in the Atg8 family of ubiquitin-like proteins and is the only protein marker described to reliably bind the autophagosomal membrane and the phagophore Method evaluation and optimization, overview
-
-
?
additional information
?
-
substrate of Renilla luciferase, coelenterazine, is a heterocyclic imidazolo-pyrazinone, which is derivatized with (4-hydroxyphenyl)methyl (R2), 4-hydroxyphenyl (R6), and phenyl-methyl (R8) moieties
-
-
?
additional information
?
-
-
8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo-[1,2-a]pyrazin-3 (7H)-one is similar to, and as active as Renilla luciferin, the native luciferin has the benzyl group replaced by an unidentified group of approximately 200 Da
-
-
?
additional information
?
-
-
native 8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo[1,2-a]pyrazin-3(7H)-one and its derivatives are most promising substrates for use with Renilla luciferin reporter enzyme in cell culture and living animals
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coelenterazine + O2
coelenteramide + CO2 + hv
-
-
-
?
coelenterazine h + O2
excited coelenteramide h monoanion + CO2
CAA01908.1
-
-
-
?
Renilla luciferin + O2
oxidized Renilla luciferin + CO2 + hv
-
-
-
-
?
coelenterazine h + O2
excited coelenteramide h monoanion + CO2
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dimethyl sulfoxide
competitive inhibition at 16.6-66 mM, binding structure analysis by circular dichroism and fluorescence spectroscopy. Seven DMSO molecules interact with amino acids onthe surface of Renilla luciferase. Two of them interact with two catalytic residues (Glu144, His285), the rest of the DMSO molecules have specific interactions with the residues in the substrate binding site including Pro220, Phe180, and Phe261
Isopropanol
compatitive inhibition at 19.3-76 mM, binding structure analysis by circular dichroism and fluorescence spectroscopy. Four isopropanol molecules interact with amino acids. Most of these molecules move around the amino acidin the binding sites, and only one isopropanol molecule interacts with His285
(2Z)-3-[[4-(dimethylamino)cyclohexa-1,5-dien-1-yl]amino]-1-phenylprop-2-en-1-one
-
-
(3Z)-3-[[4-(dimethylamino)phenyl]methylidene]-1,3-dihydro-2H-indol-2-one
-
common name SU4312
2-(4-ethoxyphenyl)-4-[(4-pyridin-2-ylpiperazin-1-yl)carbonyl]quinoline
-
-
2-(4-methylphenyl)-4-[(4-pyrimidin-2-ylpiperazin-1-yl)carbonyl]quinoline
-
-
2-hydroxy-N'-[(1E)-(2-hydroxyphenyl)methylidene]benzohydrazide
-
common name SCS
4-(1,4-dioxa-8-azaspiro[4.5]dec-8-ylcarbonyl)-2-(4-ethoxyphenyl)quinoline
-
-
4-amino-6-[(E)-[4'-[(Z)-(8-amino-1-hydroxy-5,7-disulfonato-6,7-dihydronaphthalen-2-yl)diazenyl]-3-methylbiphenyl-4-yl]diazenyl]-5-hydroxy-2,3-dihydronaphthalene-1,3-disulfonate
-
common name Evans Blue
4-[1-(1,3-benzothiazol-2-yl)-2-(4-methylpiperazin-1-yl)-2-oxoethyl]phenol
-
-
ethyl 4-[[2-(4-ethoxyphenyl)quinolin-4-yl]carbonyl]piperazine-1-carboxylate
-
-
glycerol
CAA01908.1
Renilla luciferase activity decreases at 0.8 and 1.2 M of glycerol through the obstruction of enzyme emitter site
N'-(3-chlorophenyl)-N-[(1Z)-(3-chlorophenyl)methylidene]imidoformamide
-
common name DCB
N-benzyl-4-methylbenzenesulfonamide
-
inhibition of purified enzyme, inducing activity in cell-based assay
additional information
the changes of activity of Renilla luciferase in the presence of low concentrations of small organic molecules is not associated with structural collapse or severe changes in the enzyme conformation. Molecular dynamics simulations indicate that DMSO and isopropanol, as probing molecules, aare both able to bind to the emitter site and remain with the residues of the emitter site
-
additional information
-
structure-activity relationship of luciferase inhibitors determined by quantitative high-throughput screening. Comparison of effect on various luciferase-based detection reagents
-
additional information
-
loss of enzymatic activity when in contact with substrate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bovine serum albumin
-
addition to reaction mixture enhances luciferase activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0039
coelenterazine h
pH 7.8, 25°C, recombinant His-tagged enzyme
0.00293
coelenterazine
pH 7.2, 37°C, recombinant engineered mutant super RLuc 8
0.0031
coelenterazine
pH 7.8, 25°C, recombinant His-tagged wild-type enzyme
0.0068 - 0.0103
coelenterazine
pH 7.8, 25°C, recombinant His-tagged wild-type enzyme in presence of 13.3-26.7 mM 1-butyl-3-methylimidazolium tetrafluoroborate
0.00728
coelenterazine
pH 7.2, 37°C, recombinant modified enzyme C-SRLuc8
0.0097 - 0.0119
coelenterazine
pH 7.8, 25°C, recombinant His-tagged wild-type enzyme in presence of 4.8-9.7 mM 1-butyl-3-methylimidazoliumhexafluorophosphate
0.00997
coelenterazine
pH 7.2, 37°C, recombinant wild-type enzyme SRLuc8
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
effects of trehalose and sucrose as chemical chaperones on the kinetic stability of Rluc, activity of the enzyme in presence of these additives at high temperatures, mechanism of stability, molecular dynamic simulation, modeliing, overview
-
additional information
additional information
-
effects of trehalose and sucrose as chemical chaperones on the kinetic stability of Rluc, activity of the enzyme in presence of these additives at high temperatures, mechanism of stability, molecular dynamic simulation, modeliing, overview
-
additional information
additional information
enzyme kinetics in presence and absence of imidazolium-based ionic liquids, overview
-
additional information
additional information
enzyme kinetics in presence of inhibitors DMSO and isopropanol, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
coelenterazine
-
value 111 micromol/min/micromol enzyme
additional information
additional information
-
turnover number of luciferin-analogues
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.1
dimethyl sulfoxide
pH 7.8, 25°C, recombinant His-tagged enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
(2Z)-3-[(2-bromophenyl)amino]-1-pyridin-2-ylprop-2-en-1-one
Renilla reniformis
-
IC50 above 0.05 mM
0.025
2-(4-ethoxyphenyl)-4-[(4-methylpiperazin-1-yl)carbonyl]quinoline
Renilla reniformis
-
IC50 above 0.025 mM
0.025
2-(4-methylphenyl)-4-[(4-pyrimidin-2-ylpiperazin-1-yl)carbonyl]quinoline
Renilla reniformis
-
IC50 above 0.025 mM
0.05
2-[5-(3-chlorophenyl)-1,2,4-oxadiazol-3-yl]pyridine
Renilla reniformis
-
IC50 above 0.05 mM
0.01
4-amino-6-[(E)-[4'-[(Z)-(8-amino-1-hydroxy-5,7-disulfonato-6,7-dihydronaphthalen-2-yl)diazenyl]-3-methylbiphenyl-4-yl]diazenyl]-5-hydroxy-2,3-dihydronaphthalene-1,3-disulfonate
Renilla reniformis
-
-
0.05
N'-(3-chlorophenyl)-N-[(1Z)-(3-chlorophenyl)methylidene]imidoformamide
Renilla reniformis
-
IC50 above 0.05 mM
0.011
(2Z)-3-[[4-(dimethylamino)cyclohexa-1,5-dien-1-yl]amino]-1-phenylprop-2-en-1-one
Renilla reniformis
-
-
0.011
(2Z)-3-[[4-(dimethylamino)cyclohexa-1,5-dien-1-yl]amino]-1-phenylprop-2-en-1-one
Renilla reniformis
-
pH 7.2, 22°C
0.019
(3Z)-3-[[4-(dimethylamino)phenyl]methylidene]-1,3-dihydro-2H-indol-2-one
Renilla reniformis
-
-
0.019
(3Z)-3-[[4-(dimethylamino)phenyl]methylidene]-1,3-dihydro-2H-indol-2-one
Renilla reniformis
-
pH 7.2, 22°C
0.011
2-(4-ethoxyphenyl)-4-[(4-pyridin-2-ylpiperazin-1-yl)carbonyl]quinoline
Renilla reniformis
-
-
0.011
2-(4-ethoxyphenyl)-4-[(4-pyridin-2-ylpiperazin-1-yl)carbonyl]quinoline
Renilla reniformis
-
pH 7.2, 22°C
0.02
2-hydroxy-N'-[(1E)-(2-hydroxyphenyl)methylidene]benzohydrazide
Renilla reniformis
-
pH 7.2, 22°C
0.011
4-(1,4-dioxa-8-azaspiro[4.5]dec-8-ylcarbonyl)-2-(4-ethoxyphenyl)quinoline
Renilla reniformis
-
-
0.011
4-(1,4-dioxa-8-azaspiro[4.5]dec-8-ylcarbonyl)-2-(4-ethoxyphenyl)quinoline
Renilla reniformis
-
pH 7.2, 22°C
0.0225
4-[1-(1,3-benzothiazol-2-yl)-2-(4-methylpiperazin-1-yl)-2-oxoethyl]phenol
Renilla reniformis
-
-
0.0225
4-[1-(1,3-benzothiazol-2-yl)-2-(4-methylpiperazin-1-yl)-2-oxoethyl]phenol
Renilla reniformis
-
pH 7.2, 22°C
0.02
ethyl 4-[[2-(4-ethoxyphenyl)quinolin-4-yl]carbonyl]piperazine-1-carboxylate
Renilla reniformis
-
-
0.02
ethyl 4-[[2-(4-ethoxyphenyl)quinolin-4-yl]carbonyl]piperazine-1-carboxylate
Renilla reniformis
-
pH 7.2, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
activity range, purified enzyme in absence of trehalose or sucrose
20 - 60
activity range, purified enzyme in presence of 1.2 M trehalose or sucrose
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
a collapse of alpha/beta hydrolase fold domain may trigger the irreversible inactivation of the enzyme at higher temperatures. In contrast to wild-type SRLuc8, the alpha-helices in the alpha/beta hydrolase fold domain of engineered C-SRLuc8 have lower perturbations and do not collapse, while some cap domain residues have more perturbations
additional information
additional information
architecture of the emitter site in a non-binding model, overview
additional information
enzyme active site structure and ligand-receptor interactions, molecular docking. Structure analysis using crystal structure of Renilla luciferase 8 (RLuc8), a thermostable variant of RLuc, in apo-form and incomplex with its product-coelenteramide. The enzyme has a deep tunnel made up of mostly hydrophobic residues and the catalytic triad (D120, E144 and H285) is embedded at the bottom of the tunnel. Molecular dynamic simulation and molecular docking, simulation of open conformation for docking study and of of receptor-ligand complex, with ligand/substrate coelenterazine-h (ZINC2569714), after molecular docking, overview. Evaluation of the enzymes' active site in complex with coelenterazine-h. The RMSD value is moderately higher in Super RLuc8 compared with the native variant which represents the higher motion of the ligand in Super RLuc8
additional information
molecular dynamic simulation of the native RLuc based on PDB ID 2PSF, which is the crystal structure of the mutant RLuc luciferase, overview
additional information
overall structure of the MU-RLuc model involving five mutated residues, F116L, I137V, N178D, N264S and S287P, overview
additional information
the conformational changes of a main tunnel in the structure of Renilla luciferase are directly related to enzyme activity. The enzyme activity is decreased severely in the presence of ionic liquids 1-butyl-3-methylimidazolium tetrafluoroborate and 1-butyl-3-methylimidazolium hexafluorophosphate, overview. The protein-ionic liquid interactions also have impact on the structure of enzyme, where interactions of Renilla luciferase (with alpha/beta-fold) with fluorine anions causes a conformational collapse in the exposed alpha-helices. The structural distortions in Renilla luciferase in the presence of ionic liquids is started from the outer layer of the enzyme, a model which is called the alpha-shield collapse model. Molecular dynamic simulation studies, overview. The catalytic triad is formed by residues Asp120, Glu144, and His285
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LUCI_RENRE
311
0
36022
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000 - 38000
33000 - 38000
-
sedimentation equilibrium, sedimentation velocity, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 36000, modified recombinant His-tagged enzyme C-SRLuc8, SDS-PAGE
?
x * 36000, modified recombinant His-tagged enzyme super RLuc 8, SDS-PAGE
additional information
Rluc has an alpha/beta-hydrolase fold that consists of 6 helices sur-rounding the catalytic triad in the center of the enzyme. Structure analysis at 30-40°C in absence or presence of sugars, structure comparison, overview
additional information
-
Rluc has an alpha/beta-hydrolase fold that consists of 6 helices sur-rounding the catalytic triad in the center of the enzyme. Structure analysis at 30-40°C in absence or presence of sugars, structure comparison, overview
additional information
-
tendency to self-association, forming inactive dimers and higher molecular weight species
additional information
-
anaerobic luciferin binding promotes a rapid concentration-dependent aggregation of luciferase, which results in irreversible inactivation of the enzyme
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and in complex with coelenterazine,and mutant K25A/E277A. Diffraction to 1.4 A. Structures demonstrate a classic alpha/beta-hydrolase fold. The presumptive catalytic triad residues are D120, E144, and H285. Additionally determination of structure of the accessory green fluorescent protein
molecular docking simulations with the coelenterazine substrate. Two triads of residues are critical for catalysis. Putative catalytic triad residues D120, E144, and H285 bear only limited resemblance to those of aequorin. Residues N53, W121, and P220 are also involved in catalysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F116/I137V
the mutant starts to denature at 30°C, and retained its activity up to 52°C with increased solubility at 34°C and specific activity up to approximately 119%
F116L/I137V
random mutagenesis, solubility and specific activity of the mutant is higher compared to the wild-type
F116L/I137V/I75A/N178D/N264S/S287P
the thermostability effect increases, with the mutant showing approximately 10°C higher stability. The mutant shows improved tolerance for protease digestion, e.g. trypsin and proteinase and for organic solvent. The mutant enzyme retains 100% specific activity at 45°C, while the wild type loses almost all activity, and retains activity at 55°C. The specific activity is approximately 123% higher than that of the wild type
F116L/I137V/N264S/S287P
thermostability of the mutant is increased. The mutant enzyme shows denaturation at 45 to 52°C and specific activity up to approximately 150% compared with the wild type enzyme
F180Y
I75A
specific activity of I75A is 47% of that of the wild type enzyme, retains activity up to 50°C
K25A/E277A
surface mutations made with the intention that they would aid in crystallization, not involved in contacts between proteins in the crystal
M185V/K189V/V267I
site-directed mutagenesis,compared with the native RLuc, mutant super RLuc has a higher turnover number, increased light output upon expression in Arabidopsis thaliana and enhanced half-life of photon emission, super RLuc is a blue light emitting luciferase
N178D
N264S/S287P
N45C/A71C
site-directed mutagenesis at the N-terminal of the enzyme, the engineered luciferase C-SRLuc8, improvement of the stability of super Renilla luciferase 8 (SRLuc8), which is a red-emitter variety of RLuc at higher temperatures, by introduction of a disulfide bridge into its structure. Evaluation of the proper disulfide bond formation based on computational methods, structure-function analysis, overview. The kinetic stability of C-SRLuc8 increases significantly at 60°C to 70°C as compared to SRLuc8. The N45C/A71C crosslink in C-SRLuc8 is involved in a hotspot foldon which seems to be the rate-limiting step of conformational collapse at higher temperatures. Molecular dynamic simulation studies to analyze the molecular basis of the structural changes after the introduction of the disulfide bridge. Increasing the local stability of several regions at this domain significantly improves the kinetic stability of C-SRLuc8, but the disulfide bridge in C-SRLuc8 does not delay the initial temperature of enzyme inactivation. The results of the thermal inactivation at 37°C and 65°C indicate that although CSRLuc8 shows a slight increase in stability during the first thirty minutes of incubation at 37°C, C-SRLuc8 shows a significant increase in thermostability at 65°C and increased activity as compared with SRLuc8
A55T/C124A/S130A/K136R/A143M/M185V/M253L/S287L
-
selected mutations enable the protein to emit stronger bioluminescence activity and to be more stable in serum media. Mutant m-Rluc8 exhibits an enhancement in protein expression and shows a 5.6fold improvement in light output, with increased stability in serum media confirmed to last for over 5 days
P220G
-
only 4% of the initial luciferase activity of wild-type luciferase
P220L
-
only 16% of the initial luciferase activity of wild-type luciferase
additional information
N178D
random mutagenesis, solubility and specific activity of the mutant is higher compared to the wild-type
N178D
mutation does not affect thermostability but increases the solubility at 34°C and specific activity up to approximately 141%
N264S/S287P
random mutagenesis, solubility and specific activity of the mutant is higher compared to the wild-type
N264S/S287P
the mutant starts to denature at 40°C and retains its activity up to 50°C with increased solubility at 34°C and specific activity up to approximately 150%
additional information
enzyme engineering of blue light emitting enzyme mutant super RLuc to construct a luciferase with desired light emission wavelength and thermostability, namely super RLuc8, which has a red-shifted spectrum and shows stable light emission. Super RLuc8 shows a 10fold increase in thermostability at 37°C after 20 min incubation, in comparison to the native enzyme. The optimum temperature of the mutant increases from 30 to 37°C. Molecular dynamics simulation analysis indicates that the increased thermostability is most probably caused by a better structural compactness and more local rigidity in the regions out of the emitter site. The mutant super RLuc8 shows increased activity compared t the wild-type. Molecular dynamics simulation, overview
additional information
overall structure of the MU-RLuc model involving five mutated residues, F116L, I137V, N178D, N264S and S287P, overview
additional information
stabilization of luciferase from Renilla reniformis using random mutations
additional information
super RLuc8 is a Renilla luciferase variant in which 16 amino acids are substituted
additional information
the enzyme is fused to wild-type LC3 protein and LC3 mutant G120A. LC3-II turnover is used as a marker of autophagic flux. The Rluc-LC3 fusion protein is used for the indirect autophagy flux assay based on monitoring the degradation of an autophagosome-associated fusion protein Rluc-LC3 by luminescence detection. The Rluc-LC3 assay is useful for the identification of genes, miRNAs, and small molecules that regulate autophagy flux in mammalian cells. Design of the RLUC-LC3wt and RLUC-LC3G120A fusion proteins, recombinantly expressed in MCF-7 cells. Method evaluation and optimization, overview
additional information
-
functional enzyme secreted by mammalian cells due to fusion to the signal peptide of human interleukin-2
additional information
-
mutation Cys152Ala in fusion to signal peptide of human interleukin-2 stabilizes
additional information
-
analysis of the Hsp90 chaperone activity in complex with cochaperone Cdc37 using split Renilla luciferase protein fragment-assisted complementation bioluminescence, full-length human Hsp90-Cdc37 complex and critical residues contributing to Hsp90/Cdc37 interaction in living cells, computational modeling and molecular dynamics simulations, overview. Cysteines at the N-terminus of Cdc37 do not directly contribute to Hsp90-Cdc37 complex formation
additional information
-
method development of Renilla luciferase used in an assay for measurement of mitochondrial fusion, quantification via split-Renilla luciferase complementation in HeLa cells, overview
additional information
-
substitution of the V3 region of the multifunctional NS5A protein of hepatitis C virus FH1 with the Renilla reniformis luciferase Rluc gene. The deletion of the V3 region from the genome does only slightly affect the titer of infectious virus produced in human hepatoma cell line, Huh 7.5. The transfected virus stably expresses an NS5A-Rluc fusion protein, kinetics of virus production, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Rluc remaining activity in the absence and presence of 0.6 M and 1.2 M of trehalose, and 1.2 M of sucrose at 30°C is 15%, about 50%, around 100%, and almost 60%, respectively, after 60 min
30 - 52
the F116L/I137V mutant shows a transition starting at 30°C, which is 5°C lower than the wild-type, and ending at 52°C, which is 5°C higher than the wild type. N178D mutant has almost the same denaturation profile
35 - 47
purified recombinant His-tagged wild-type RLuc retains full activity up to 35°C and is inactivated at 47°C
37
40
in the absence and presence of 0.6 M of trehalose, the remaining activity is only about 2% and 6%, respectively, although it increases about 70fold upon incubation of the enzyme solution in a buffer containing 1.2 M of trehalose. It also seems that the remaining activity in the presence of 1.2 M of sucrose in the first 10 min is slightly better than in its absence, and a little activity is seen even after 60 min
40 - 47
the stability of the purified recombinant His-tagged N264S/S287P mutant is maintains at a temperature that is 5°C higher than the wild-type.
45
pH 7.8, the activity of purified recombinant His-tagged engineered mutant superRLuc8 remains around 60% after incubation at 45°C, while wild-type recombinant His-tagged RLuc loses approximately 82% of its initial activity at the same temperature
50 - 70
engineered enzyme C-SRLuc8 shows significant stability, retaining about 20% of its initial activity after incubation at 70°C for 5 min, while wild-type SRLuc8 completely loses its activity after incubation at this temperature
65
the residual activity of modified enzyme C-SRLuc8 is approximately 20% after incubation at 65°C for 5 min
37
C-SRLuc8 and SRLuc8 start to collapse at temperatures close to 37°C
37
pH 7.8, 60 min, 4 and 10fold increases in recombinant His-tagged engineered super RLuc8 thermostability are observed at 37°C after 10 and 20 min incubation, respectively, in comparison to the recombinant His-tagged wild-type enzyme. While the wild-type enzyme is completely inactivated after 30 min, the mutant enzyme retains about 30% of its initial activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
trehalose a thermostabilizing effect, a wide radial like network of trehalose molecules supports alpha-helix structures that are located in the N-terminus and C-terminus of the protein. In the water simulation box, these helices alter to instable structures at high temperatures. Reduction of the fluctuation of these helices in the presence of trehalose molecules, may prevent the protein from unfolding and increase its shelf-life
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-propanol
10%, residual activity of the mutant after treatment is 29.4%, residual activity of the wild type enzyme is 0.4%
dimethylformamide
10%, residual activity of the mutant after treatment is 24.8%, residual activity of the wild type enzyme is 0.1%
DMSO
10%, residual activity of the mutant after treatment is 91.3%, residual activity of the wild type enzyme is 24.3%
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
anaerobic luciferin binding promotes a rapid concentration-dependent aggregation of luciferase, which results in irreversible inactivation of the enzyme
-
439337
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged engineered enzyme C-SRLuc8 in Escherichia coli by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography to over 95% purity
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant soluble His6-tagged enzyme FcUni-RLuc from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of stabilized variant RLuc8 with noncleavable N-terminal His6-tag
gene luc, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of engineered His-tagged enzyme C-SRLuc8 in Escherichia coli, method optimization
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 Star (DE3)
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of soluble His6-tagged enzyme FcUni-RLuc in Escherichia coli strain BL21 (DE3), an Fc-binding peptide is separated by a five-amino acid linker from RLuc
expressed as a soluble form in Escherichia coli BL21(DE3)pLysS (Novagen) containing the expression vector pET-21a inserted with cDNA of Renilla luciferase
CAA01908.1
expressed using a cold-induced expression system in Escherichia coli as His-tagged fusion proteins
-
expression of Renilla luciferase split fragments in HeLa cells, mitochondrial localization, overview
-
fragments of Renilla luciferase (Rluc) are fused to the chemotaxis-associated response regulator CheY3 and its phosphatase CheZ in the enteric pathogen Vibrio cholerae in order to demonstrate dynamic protein-protein interactions by luciferase complementation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
an advanced Fc-binding probe, FcUni-RLuc, is produced and functionally assayed for labelling IgGs. The Fc antibody binding sequence HWRGWV is fused to Renilla luciferase, and the purified probe is employed for bioluminescence enzyme-linked immunoabsorbance assay of Her2 positive cells
diagnostics
molecular biology
analysis
biotechnology
molecular biology
-
dual luciferase enzyme assay system for reporter gene analysis combining both the firefly luciferase enzyme and the Renilla luciferase enzyme in a nonproprietary buffer
analysis
an advanced Fc-binding probe, FcUni-RLuc, is produced and functionally assayed for labelling IgGs. The Fc antibody binding sequence HWRGWV is fused to Renilla luciferase, and the purified probe is employed for bioluminescence enzyme-linked immunoabsorbance assay of Her2 positive cells
analysis
establishment and evaluation of an indirect autophagy flux assay based on monitoring the degradation of an autophagosome-associated fusion protein Rluc-LC3 by luminescence detection. The Rluc-LC3 assay is useful for the identification of genes, miRNAs, and small molecules that regulate autophagy flux in mammalian cells
analysis
Renilla luciferase is a bioluminescent enzyme which is broadly used as a reporter protein in molecularbiosensors
diagnostics
Renilla Luciferase (RLuc) is a blue light emitter protein which can be applied as a valuable tool in medical diagnosis
diagnostics
the split Renilla luciferase complementation assay (SRLCA) is one of the techniques that detect protein-protein interactions. The SRLCA is based on the complementation of the LN and LC non-functional halves of Renilla luciferase fused to possibly interacting proteins which after interaction form a functional enzyme and emit luminescence. The SRLCA can specifically detect the BGLF4/Hsp90 interaction and provide a reference to develop inhibitors that disrupt the Epstein-Barr virus kinase BGLF4 and heat shock protein Hsp90 interaction
diagnostics
the enzyme is a good research tool as a reporter protein and bioimaging probes, yielding blue light using the substrate coelenterazine. However the applications are limited since RLuc is unstable under various conditions
molecular biology
an advanced Fc-binding probe, FcUni-RLuc, is produced and functionally assayed for labelling IgGs. The Fc antibody binding sequence HWRGWV is fused to Renilla luciferase, and the purified probe is employed for bioluminescence enzyme-linked immunoabsorbance assay of Her2 positive cells
molecular biology
Renilla luciferase (Rluc) from Renilla reniformis is an appropriate protein reporter for the detection of specific molecular targets due to its bioluminescent feature, although its relatively low stability limits the application
analysis
-
analysis of luciferase inhibitors by quantitative high-throughput screening and comparison of and structure-activity relationship using various luciferase-based detection reagents
analysis
-
development of a bioluminiscent probe composed of peptide EYFP and luciferase for near-real-time single-cell imaging using bioluminescence resonance energy transfer BRET. The probe exhibits enhanced luciferase luminescence intensity and appropriate subcellular distribution when it is fused to targeting-signal peptides or histone H2AX. It allows high spatial and temporal resolution microscopy of living cells
analysis
-
the use of control Renilla luciferase vectors as normalizers requires that they not be influenced by any variables in the experiment. The zinc finger transcription factor WT1 effect on luciferase activation varies from no significant effect in 293 and PC3 cells to strong enhancement in LNCaP cells treated with the androgen analog R1881. Hormone enhances WT1-mediated activation of luciferase and these interactions require an intact WT1 zinc finger DNA binding domain
analysis
-
for analysis of the Hsp90 chaperone activity in complex with cochaperone Cdc37, split Renilla luciferase protein fragment-assisted complementation bioluminescence can be utilized to study the full-length human Hsp90-Cdc37 complex and to identity critical residues and their contributions for Hsp90/Cdc37 interaction in living cells
analysis
-
Renilla luciferase is used in assay development for measurement of mitochondrial fusion, quantification via split-Renilla luciferase complementation in HeLa cells, validation of the Renilla luciferase reporter system for mitochondrial fusion, overview
biotechnology
-
expression of native gene and commercial synthetic gene, optimized for expression, in several cell lines and in mouse. Use of synthetic gene as primary reporter gene with high sensitivity in living rodents
biotechnology
-
use of enzyme as a reporter is dependent on the promotor driving its expression, the presence of co-transfected transgenes, and the androgen responsiveness of the cell line used
biotechnology
-
use of native coelenterazine and its derivatives e, -f, -h, as substrates for use in cell culture and living animals
biotechnology
-
popular reporter enzyme for gene expression and biosensor applications
biotechnology
-
split luciferase complementation is applied to study dynamic protein-protein interactions in live bacteria. Nonspecific inhibition of Rluc activity by small molecule effectors compromises the utility of this technique in measuring dynamic protein-protein interactions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cormier, M.J.; Hori, K.; Anderson, J.M.
Bioluminescence in coelenterates
Biochim. Biophys. Acta
346
137-164
1974
Renilla koellikeri, Renilla muelleri, Renilla reniformis
Matthews, J.C.; Hori, K.; Cormier, M.J.
Purification and properties of Renilla reniformis luciferase
Biochemistry
16
85-91
1977
Renilla reniformis
DeLuca, M.; Dempsey, M.E.; Hori, K.; Wampler, J.E.; Cormier, M.J.
Mechanism of oxidative carbon dioxide production during Renilla reniformis bioluminescence
Proc. Natl. Acad. Sci. USA
68
1658-1660
1971
Renilla reniformis
Hart, R.C.; Matthews, J.C.; Hori, K.; Cormier, M.J.
Renilla reniformis bioluminescence: luciferase-catalyzed production of nonradiating excited states from luciferin analogues and elucidation of the excited state species involved in energy transfer to Renilla green fluorescent protein
Biochemistry
18
2204-2210
1979
Renilla reniformis
Matthews, J.C.; Hori, K.; Cormier, M.J.
Substrate and substrate analogue binding properties of Renilla luciferase
Biochemistry
16
5217-5220
1977
Renilla reniformis
Karkhanis, Y.D.; Cormier, M.J.
Isolation and properties of Renilla reniformis luciferase, a low molecular weight energy conversion enzyme
Biochemistry
10
317-326
1971
Renilla reniformis
Liu, J.; Escher, A.
Improved assay sensitivity of an engineered secreted Renilla luciferase
Gene
237
153-159
1999
Renilla reniformis
Liu, J.; O'Kane, D.J.; Escher, A.
Secretion of functional Renilla reniformis luciferase by mammalian cells
Gene
203
141-148
1997
Renilla reniformis
Bhaumik, S.; Lewis, X.Z.; Gambhir, S.S.
Optical imaging of Renilla luciferase, synthetic Renilla luciferase, and firefly luciferase reporter gene expression in living mice
J. Biomed. Opt.
9
578-586
2004
Renilla reniformis
Zhao, H.; Doyle, T.C.; Wong, R.J.; Cao, Y.; Stevenson, D.K.; Piwnica-Worms, D.; Contag, C.H.
Characterization of coelenterazine analogs for measurements of Renilla luciferase activity in live cells and living animals
Mol. Imaging
3
43-54
2004
Renilla reniformis
Mulholland, D.J.; Cox, M.; Read, J.; Rennie, P.; Nelson, C.
Androgen responsiveness of Renilla luciferase reporter vectors is promoter, transgene, and cell line dependent
Prostate
59
115-119
2004
Renilla reniformis
Dyer, B.W.; Ferrer, F.A.; Klinedinst, D.K.; Rodriguez, R.
A noncommercial dual luciferase enzyme assay system for reporter gene analysis
Anal. Biochem.
282
158-161
2000
Renilla reniformis
Hanson, J.; Reese, J.; Gorman, J.; Cash, J.; Fraizer, G.
Hormone treatment enhances WT1 activation of renilla luciferase constructs in LNCaP cells
Front. Biosci.
12
1387-1394
2007
Renilla reniformis
Auld, D.S.; Southall, N.T.; Jadhav, A.; Johnson, R.L.; Diller, D.J.; Simeonov, A.; Austin, C.P.; Inglese, J.
Characterization of chemical libraries for luciferase inhibitory activity
J. Med. Chem.
51
2372-2386
2008
Renilla reniformis
Loening, A.M.; Fenn, T.D.; Gambhir, S.S.
Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis
J. Mol. Biol.
374
1017-1028
2007
Renilla reniformis (P27652)
Hoshino, H.; Nakajima, Y.; Ohmiya, Y.
Luciferase-YFP fusion tag with enhanced emission for single-cell luminescence imaging
Nat. Methods
4
637-639
2007
Renilla reniformis
Woo, J.; Howell, M.H.; von Arnim, A.G.
Structure-function studies on the active site of the coelenterazine-dependent luciferase from Renilla
Protein Sci.
17
725-735
2008
Renilla reniformis (P27652)
Woo, J.; v. Arnim, A.G.
Mutational optimization of the coelenterazine-dependent luciferase from Renilla
Plant Methods
4
23
2008
Renilla reniformis
Auld, D.S.; Thorne, N.; Maguire, W.F.; Inglese, J.
Mechanism of PTC124 activity in cell-based luciferase assay of nonsense codon suppression
Proc. Natl. Acad. Sci. USA
106
3585-3590
2009
Renilla reniformis
Liu, S.; Nelson, C.A.; Xiao, L.; Lu, L.; Seth, P.P.; Davis, D.R.; Hagedorn, C.H.
Measuring antiviral activity of benzimidazole molecules that alter IRES RNA structure with an infectious hepatitis C virus chimera expressing Renilla luciferase
Antiviral Res.
89
54-63
2010
Renilla reniformis
Jiang, Y.; Bernard, D.; Yu, Y.; Xie, Y.; Zhang, T.; Li, Y.; Burnett, J.P.; Fu, X.; Wang, S.; Sun, D.
Split Renilla luciferase protein fragment-assisted complementation (SRL-PFAC) to characterize Hsp90-Cdc37 complex and identify critical residues in protein/protein interactions
J. Biol. Chem.
285
21023-21036
2010
Renilla reniformis
Huang, H.; Choi, S.Y.; Frohman, M.A.
A quantitative assay for mitochondrial fusion using Renilla luciferase complementation
Mitochondrion
10
559-566
2010
Renilla reniformis
Hatzios, S.; Ringgaard, S.; Davis, B.; Waldor, M.
Studies of dynamic protein-protein interactions in bacteria using renilla luciferase complementation are undermined by nonspecific enzyme inhibition
PLoS ONE
7
e43175
2012
Renilla reniformis
Inouye, S.; Sahara-Miura, Y.; Sato, J.; Iimori, R.; Yoshida, S.; Hosoya, T.
Expression, purification and luminescence properties of coelenterazine-utilizing luciferases from Renilla, Oplophorus and Gaussia: comparison of substrate specificity for C2-modified coelenterazines
Protein Expr. Purif.
88
150-156
2013
Oplophorus gracilirostris, Renilla reniformis, Gaussia
Song, W.C.; Sung, H.J.; Park, K.S.; Choi, J.W.; Cho, J.Y.; Um, S.H.
Novel functional Renilla luciferase mutant provides long-term serum stability and high luminescence activity
Protein Expr. Purif.
91
215-220
2013
Renilla reniformis
Wang, J.; Guo, W.; Long, C.; Zhou, H.; Wang, H.; Sun, X.
The split Renilla luciferase complementation assay is useful for identifying the interaction of Epstein-Barr virus protein kinase BGLF4 and aheat shock protein Hsp90
Acta Virol.
60
62-70
2016
Renilla reniformis (P27652)
Farzannia, A.; Roghanian, R.; Zarkesh-Esfahani, S.H.; Nazari, M.; Emamzadeh, R.
FcUni-RLuc an engineered Renilla luciferase with Fc binding ability and light emission activity
Analyst
140
1438-1441
2015
Renilla reniformis (P27652)
Ghaedizadeh, S.; Emamzadeh, R.; Nazari, M.; Rasa, S.; Zarkesh-Esfahani, S.; Yousefi, M.
Understanding the molecular behaviour of Renilla luciferase in imidazolium-based ionic liquids, a new model for the alpha/beta fold collapse
Biochem. Eng. J.
105
505-513
2016
Renilla reniformis (P27652)
-
Fanaei Kahrani, Z.; Emamzadeh, R.; Nazari, M.; Rasa, S.M.
Molecular basis of thermostability enhancement of Renilla luciferase at higher temperatures by insertion of a disulfide bridge into the structure
Biochim. Biophys. Acta
1865
252-259
2017
Renilla reniformis (P27652)
Rahnama, S.; Saffar, B.; Kahrani, Z.F.; Nazari, M.; Emamzadeh, R.
Super RLuc8 A novel engineered Renilla luciferase with a red-shifted spectrum and stable light emission
Enzyme Microb. Technol.
96
60-66
2017
Renilla reniformis (P27652)
Salehi, F.; Emamzadeh, R.; Nazari, M.; Rasa, S.M.
Probing the emitter site of Renilla luciferase using small organic molecules; an attempt to understand the molecular architecture of the emitter site
Int. J. Biol. Macromol.
93
1253-1260
2016
Renilla reniformis (P27652)
Liyaghatdar, Z.; Emamzadeh, R.; Rasa, S.M.M.; Nazari, M.
Trehalose radial networks protect Renilla luciferase helical layers against thermal inactivation
Int. J. Biol. Macromol.
105
66-73
2017
Renilla reniformis (P27652), Renilla reniformis
Kahrani, Z.F.; Ganjalikhany, M.R.; Rasa, S.M.M.; Emamzadeh, R.
New Insights into the Molecular characteristics behind the function of Renilla luciferase
J. Cell. Biochem.
119
1780-1790
2018
Renilla reniformis (P27652)
Farkas, T.; Jaeaettelae, M.
Renilla luciferase-LC3 based reporter assay for measuring autophagic flux
Methods Enzymol.
588
1-13
2017
Renilla reniformis (P27652)
Jiang, T.; Yang, X.; Yang, X.; Yuan, M.; Zhang, T.; Zhang, H.; Li, M.
Novel bioluminescent coelenterazine derivatives with imidazopyrazinone C-6 extended substitution for Renilla luciferase
Org. Biomol. Chem.
14
5272-5281
2016
Renilla reniformis (P27652)
Shigehisa, M.; Amaba, N.; Arai, S.; Higashi, C.; Kawanabe, R.; Matsunaga, A.; Laksmi, F.A.; Tokunaga, M.; Ishibashi, M.
Stabilization of luciferase from Renilla reniformis using random mutations
Protein Eng. Des. Sel.
30
7-13
2017
Renilla reniformis (P27652)
Khoshnevisan, G.; Emamzadeh, R.; Nazari, M.; Rasa, S.M.M.; Sariri, R.; Hassani, L.
Kinetics, structure, and dynamics of Renilla luciferase solvated in binary mixtures of glycerol and water and the mechanism by which glycerol obstructs the enzyme emitter site
Int. J. Biol. Macromol.
117
617-624
2018
Renilla reniformis (CAA01908.1)
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