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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
-
-
-
-
?
2-benzyl-3-[(2-nitrophenyl)methoxy]-6-phenyl-8-(phenylsulfanyl)imidazo[1,2-a]pyrazine + O2
? + CO2
Renilla sp.
-
the substrate presents robust bioluminescent signals ex vivo and in living animals after UV irradiation at 365 nm
-
-
?
2-benzyl-3-[(4,5-dimethoxy-2-nitrophenyl)methoxy]-6-phenyl-8-(phenylsulfanyl)imidazo[1,2-a]pyrazine + O2
? + CO2
Renilla sp.
-
the substrate presents robust bioluminescent signals ex vivo and in living animals after UV irradiation at 365 nm
-
-
?
2-benzyl-3-[1-(2-nitrophenyl)ethoxy]-6-phenyl-8-(phenylsulfanyl)imidazo[1,2-a]pyrazine + O2
? + CO2
Renilla sp.
-
the substrate presents robust bioluminescent signals ex vivo and in living animals after UV irradiation at 365 nm
-
-
?
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
-
-
-
?
2-hydroperoxycoelenterazine + O2
?
-
-
-
?
3iso-coelenterazine + O2
?
3me-coelenterazine + O2
?
3meo-coelenterazine + O2
?
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
-
-
-
-
?
alphameh-coelenterazine + O2
?
b-coelenterazine + O2
?
Renilla sp.
-
-
-
-
?
beetle D-luciferin
?
-
450 microM
-
-
?
benzylluciferin + O2
oxidized benzylluciferin + CO2 + hv
-
-
-
-
?
benzylluciferin methyl ether + O2
oxidized benzylluciferin methyl ether + CO2 + hv
-
-
-
-
?
bis-coelenterazine + O2
hnu + ?
-
assay at pH 7.6, about 100fold reduced relative luminescence
-
-
?
cf3-coelenterazine + O2
?
coelenterate-type luciferin + O2
oxidized coelenterate-type luciferin + CO2 + hv
-
-
-
-
?
coelenterazine + ?
?
-
20 microM
-
-
?
coelenterazine + O2
? + CO2 + hv
-
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hnu
coelenterazine + O2
coelenteramide + CO2 + hv
coelenterazine + O2
oxidized coelenterazine + CO2 + hn
-
-
-
-
?
coelenterazine h + O2
coelenteramide h + CO2 + hv
-
-
-
?
coelenterazine h + O2
excited coelenteramide h monoanion + CO2
coelenterazine-h + O2
coelenteramide h + CO2 + hv
substrate binding structure
-
-
?
coelenterazine-v + O2
coelenteramide-v + CO2 + hnu
increase of substrate coelenterazine stability by ligating it to Ca2+-triggered coelenterazine-binding protein, CBP, from Renilla muelleri, which apparently functions in the organism for stabilizing and protecting coelenterazine from oxidation. The apo-CBP binds coelenterazine-v very rapidly from Ca2+ free solution, similar to that as the native coelenterazine. At low concentrations, coelenterazine-v bound within CBP generates a brighter bioluminescence signal than would free coelenterazine, thereby increasing the assay sensitivity, overview
orange bioluminescence
-
?
coelentrazine + O2
?
-
-
-
?
cp-coelenterazine + O2
hnu + ?
-
assay at pH 7.6, about 100fold reduced relative luminescence
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
e-coelenterazine + O2
hnu + ?
-
assay at pH 7.6, about 100fold reduced relative luminescence
-
-
?
f-coelenterazine + O2
hnu + ?
-
assay at pH 7.6, about 100fold reduced relative luminescence
-
-
?
fcp-coelenterazine + O2
hnu + ?
-
assay at pH 7.6, about 100fold reduced relative luminescence
-
-
?
h-coelenterazine + O2
hnu + ?
-
assay at pH 7.6m, about 100fold reduced relative luminescence
-
-
?
hcp-coelenterazine + O2
hnu + ?
-
assay at pH 7.6, about 100fold reduced relative luminescence
-
-
?
luciferin + O2
?
-
assay at pH 7.4, 25-30°C, 10 min
-
-
?
meo-coelenterazine + O2
?
MeO-coelenterazine + O2
hnu + ?
-
assay at pH 7.6, about 100fold reduced relative luminescence
-
-
?
methyl luciferin + O2
?
-
-
-
-
?
n-coelenterazine + O2
hnu + ?
-
assay at pH 7.6, about 100fold reduced relative luminescence
-
-
?
Renilla luciferin + O2
oxidized Renilla luciferin + CO2 + hv
additional information
?
-
3iso-coelenterazine + O2
?
-
relative activity to native coelenterazine: 14.3%
-
-
?
3iso-coelenterazine + O2
?
-
relative activity to native coelenterazine: 78.2%
-
-
?
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: 2.6%
-
-
?
3me-coelenterazine + O2
?
-
relative activity to native coelenterazine: 80%
-
-
?
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: 3.8%
-
-
?
3meo-coelenterazine + O2
?
-
relative activity to native coelenterazine: 189%
-
-
?
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: 15.7%
-
-
?
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: 0.8%
-
-
?
cf3-coelenterazine + O2
?
-
relative activity to native coelenterazine: 49.5%
-
-
?
cf3-coelenterazine + O2
?
-
relative activity to native coelenterazine: 16.8%
-
-
?
cf3-coelenterazine + O2
?
-
relative activity to native coelenterazine: 5%
-
-
?
coelenterazine + O2
?
-
-
-
-
?
coelenterazine + O2
?
-
relative activity: 100%
-
-
?
coelenterazine + O2
?
-
-
-
-
?
coelenterazine + O2
?
0.1 mM
-
-
?
coelenterazine + O2
?
-
20 microM, assay at pH 8.0
-
-
?
coelenterazine + O2
?
-
relative activity: 100%
-
-
?
coelenterazine + O2
?
-
relative activity: 100%
-
-
?
coelenterazine + O2
?
-
assay at pH 7.2
-
-
?
coelenterazine + O2
?
Renilla sp.
-
-
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hnu
-
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hnu
-
0.5 microg, assay at pH 7.6, high substrate specificity for coelenterazine
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hnu
-
assay at pH 7.4, 25-30°C, 10 min
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hnu
the enzyme catalyzes the oxidative decarboxylation of coelenterazine in the presence of O2, resulting in the formation of coelenteramide in its excited state and CO2 as the reaction product
green bioluminescence
-
?
coelenterazine + O2
coelenteramide + CO2 + hnu
Renilla sp.
-
-
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hv
-
blue fluorescent protein from the calcium-binding photoprotein aequorin (BFP-aq) is a complex of Ca2+-bound apoaequorin and coelenteramide, and shows luminescence activity like a luciferase. The oxidation of coelenterazine by BFP-aq in the luciferase reaction and the regeneration process to aequorin might involve the same catalytic site of BFP-aq
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hv
-
-
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hv
-
clytin emits light on reacting with Ca2+. The Ca2+ sensitivity of recombinant clytin is lower than that of aequorin
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hv
coelenterazine is bound by coelenterazine-binding protein. In combinantion with renilla luciferase, addition of only one Ca2+-ion is sufficient to release coelenterazine as a substrate. The combination of the two proteins generates bioluminescence with higher reaction efficiency than using free coelenterazine alone
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hv
-
-
-
-
?
coelenterazine + O2
coelenteramide + CO2 + hv
-
-
-
?
coelenterazine h + O2
excited coelenteramide h monoanion + CO2
-
-
-
?
coelenterazine h + O2
excited coelenteramide h monoanion + CO2
-
-
-
-
?
coelenterazine h + O2
excited coelenteramide h monoanion + CO2
CAA01908.1
-
-
-
?
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)
-
-
?
coelenterazine-H + O2
?
-
-
-
-
?
coelenterazine-H + O2
?
-
5 microM, assay at pH 7.5
-
-
?
D-luciferin + O2
?
-
-
-
-
?
D-luciferin + O2
?
Renilla sp.
-
-
-
-
?
et-coelenterazine + O2
?
-
relative activity to native coelenterazine: 0.9%
-
-
?
et-coelenterazine + O2
?
-
relative activity to native coelenterazine: 21.1%
-
-
?
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: 5.8%
-
-
?
h-coelenterazine + O2
?
-
relative activity to native coelenterazine: 68.4%
-
-
?
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: 0.9%
-
-
?
i-coelenterazine + O2
?
-
relative activity to native coelenterazine: 32.3%
-
-
?
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: 4.5%
-
-
?
me-coelenterazine + O2
?
-
relative activity to native coelenterazine: 46.6%
-
-
?
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: 13.6%
-
-
?
meo-coelenterazine + O2
?
-
relative activity to native coelenterazine: 68.1%
-
-
?
meo-coelenterazine + O2
?
-
relative activity to native coelenterazine: 1.2%
-
-
?
meo-coelenterazine + O2
?
-
relative activity to native coelenterazine: 18.2%
-
-
?
Renilla luciferin + O2
oxidized Renilla luciferin + CO2 + hv
-
-
-
-
?
Renilla luciferin + O2
oxidized Renilla luciferin + CO2 + hv
-
-
-
-
?
Renilla luciferin + O2
oxidized Renilla luciferin + CO2 + hv
-
-
-
-
?
additional information
?
-
free coelenterazine and its analogues are unstable in neutral aqueous solution, undergoing a slow autooxidation over several hours
-
-
?
additional information
?
-
-
free coelenterazine and its analogues are unstable in neutral aqueous solution, undergoing a slow autooxidation over several hours
-
-
?
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
-
-
?
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
-
-
?
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D117G
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 5°C higher than wild-type value
D153G
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 7°C higher than wild-type value
E128G
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 2°C higher than wild-type value
E35G
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is identical to wild-type value
F149S
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 5°C lower than wild-type value
L170I
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 4°C higher than wild-type value
Q168A/L170V
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 8°C higher than wild-type value
Q168K/L170V
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 8°C higher than wild-type value
Q168R
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 9°C higher than wild-type value
Q168R/L170I
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 13°C higher than wild-type value
Q168R/L170M
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 8°C higher than wild-type value
Q168R/L170V
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 13°C higher than wild-type value
V44A
the temperature for 50% inactivation of aequorin bioluminescence by a 30-min heat shock is 1°C higher than wild-type value
DBHsp-GLuc
-
dopamine beta-hydroxlase fused to GLase, lower luminescence activity than wild-type GLuc
deltaSP-GLuc
-
GLuc without signal peptide sequence, no significant luminescence
extGLuc
-
membrane-anchored
Gluc(HPG)mutant
-
contains L-homopropargylglycine, prolonged luminescence, reduced specific activity
M43I
-
after 120 s of incubation time still 87% residual light emission compared to only 30% of wild-type Gluc, stabilized light emission with detergent Triton X-100, more stable light emission compared to wild-type Gluc when expression in mammalian cells
pCold-hGL
-
two repeat sequences, two catalytic domains
pCold-hGL-27/97
-
one repeat sequence, with only one catalytic domain
pCold-hGL-98/168
-
one repeat sequence, with only one catalytic domain
pCold-hSGL
-
with a signal peptide sequence for secretion
A55T/C124A/C130A/A143M/M253L/S287L/A123T/D154M/E155G/D162E/I163L/V185L
sequentially introduced into the RM-Luc coding sequence using designed oligonucleotide primers and quick-change site-directed mutagenesis, the mutant RM-Y has a red-shifted bioluminescence spectrum
A164W
73% of wild-type activity
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
D120E
1.1% of wild-type activity
D120F
no activity detected
D120Y
no activity detected
E144D
5.6% of wild-type activity
E144F
no activity detected
E144Y
no activity detected
E160N
27.2% of wild-type activity
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
F180C
14.3% of wild-type activity
F180T
5.4% of wild-type activity
F261A
no activity detected
F261S
no activity detected
H285A
11.3% of wild-type activity
H285D
no activity detected
H285K
no activity detected
H285N
0.1% of wild-type activity
I140L
113% of wild-type activity
I163F
11.0% of wild-type activity
I223W
0.2% of wild-type activity
I75A
specific activity of I75A is 47% of that of the wild type enzyme, retains activity up to 50°C
K189D
24.7% of wild-type activity
K189V
-
increased activity
K193S
54.8% of wild-type activity
K25A/E277A
surface mutations made with the intention that they would aid in crystallization, not involved in contacts between proteins in the crystal
K308I
47.5% of wild-type activity
M185V
-
increased activity
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
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
N53C
3.4% of wild-type activity
N53G
0.5% of wild-type activity
N53H
2.1% of wild-type activity
N53M
1.8% of wild-type activity
N53P
no activity detected
N53Q
25.1% of wild-type activity
N53R
90% of wild-type activity
N53S
20.7% of wild-type activity
P157R
101% of wild-type activity
P220C
72.7% of wild-type activity
P220E
4.9% of wild-type activity
P220F
15.7% of wild-type activity
P220M
140% of wild-type activity
P220Q
222% of wild-type activity
P220S
55.4% of wild-type activity
P220T
89.6% of wild-type activity
P220V
70.5% of wild-type activity
T184C
62.7% of wild-type activity
T184F
46.1% of wild-type activity
T329G
-
no significant influence on enzyme activity
V267I
-
increased activity
W121A
26.8% of wild-type activity
W121G
4.9% of wild-type activity
W121R
1.1% of wild-type activity
W121S
17.3% of wild-type activity
W121Y
3.1% of wild-type activity
223-224insRev
Renilla sp.
-
Rev peptide-inserted Rluc variant
223-224insTat
Renilla sp.
-
Tat peptide-inserted Rluc variant
223C/A-224insRev
Renilla sp.
-
Tat peptide-inserted Rluc variant
223C/A-224insTat
Renilla sp.
-
Tat peptide-inserted Rluc variant
229-230insRev
Renilla sp.
-
Rev peptide-inserted Rluc variant
229-230insTat
Renilla sp.
-
high thermal stability
229C/A-230insRev
Renilla sp.
-
Rev peptide-inserted Rluc variant
229C/A-230insTat
Renilla sp.
-
high thermal stability, higher enzyme activity than PI-RLuc
91-92C/AinsRev
Renilla sp.
-
higher enzyme activity than PI-RLuc
91-92insRev
Renilla sp.
-
Rev peptide-inserted Rluc variant
91-92insTat
Renilla sp.
-
higher enzyme activity than PI-RLuc
A55T/C124A/S130A/K136R/A143M/M185V/M253L/S287L
Renilla sp.
-
mutant enzyme exhibits a greater than 4-fold enhancement in activity, a 200fold increased resistance to serum inactivation, and a small but measurable 5 nm red shift in the emission spectrum. The enhancement in light output arises from a combination of increases in quantum yield and improvedkinetics
C124A
Renilla sp.
-
increased enzymatic activity, 41fold higher luminescence than wild-type luciferase
C124Ac
Renilla sp.
-
C-terminal half, decreased enzymatic activity
C124An
Renilla sp.
-
N-terminal half, decreased enzymatic activity
C126A
Renilla sp.
-
increased activity
extFLuc
Renilla sp.
-
membrane-anchored
G229stopstop
Renilla sp.
-
Rluc N-terminal fragment
M185V/Q235A
Renilla sp.
-
compared with the native enzyme the mutant has twice the rate of inactivation, as measured in murine serum, while incorporating a close to 5fold improvement in light output
N64C
Renilla sp.
-
Ca2+-induced interaction between calmodulin and M13 leads to intermolecular complementation of split Renilla luciferase, decreased enzymatic activity
RL8
Renilla sp.
-
mutant of Rluc
RLuc8
Renilla sp.
-
eight-point mutation variant of renilla luciferase
stop230
Renilla sp.
-
Rluc C-terminal fragment
F180Y
11.0% of wild-type activity
F180Y
61.8% of wild-type activity
M185G
16.7% of wild-type activity
M185G
-
slightly increased half life
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%
P220G
548% of wild-type activity
P220G
-
only 4% of the initial luciferase activity of wild-type luciferase
P220L
500% of wild-type activity
P220L
-
only 16% of the initial luciferase activity of wild-type luciferase
additional information
-
conjugate of GLuc with the IM9 protein
additional information
construct of vector with signal peptide from GLuc and gene sequence from human endostatin
additional information
-
construct of vector with signal peptide from GLuc and gene sequence from human endostatin
additional information
fusion of GLuc to a biotin acceptor peptide, attachment of a single biotin to the fusion protein mediated by the biotin protein ligase, EC 6.3.4.15
additional information
-
fusion of GLuc to a biotin acceptor peptide, attachment of a single biotin to the fusion protein mediated by the biotin protein ligase, EC 6.3.4.15
additional information
-
fusion of Gluc to fluorescent protein YFP
additional information
substitution of native Gaussia luciferase signal sequence by that from human interleukin-2 or albumin, reduced amount of protein, decreased luciferase activity
additional information
-
substitution of native Gaussia luciferase signal sequence by that from human interleukin-2 or albumin, reduced amount of protein, decreased luciferase activity
additional information
-
without the signal sequence higher enzyme yield and activity
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
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
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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
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
analysis
enhanced-sensitivity, synthetically facile reporter fusion to merge the bioluminescence output of Gaussia luciferase with the biotin-binding ability of tamavidin 2. The fusion construct enables direct bacterial expression of a reporter system incorporating two functionalities in a 1:1 stoichiometric relationship. Using a cold-shock expression system, highly concentrated construct can be obtained from standard culture volumes while retaining essentially native protein activity. The fusion construct can be included in a standard target-bridged assay design for the sensitive detection of miRNA targets
analysis
luciferase can be functionally expressed in Staphylococcus aureus and can be used as a biosensor for the agr quorum sensing system which employs autoinducing peptides to control virulence. Luciferase is linked to the P3 promoter of the agr operon and biosensor strains are validated by evaluation of chemical agent-mediated activation and inhibition of agr. Use of Luciferase enables quantitative assessment of agr activity
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
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
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
Renilla sp.
-
development of a reverse genetic model to characterize the pathway of replication and pathogenesis of the SARS coronavirus. Renilla luciferase is used as a reporter gene and inserted into the backbone of the infectious clone of SARS coronavirus to replace ORF 7a/b (SARS wt-Luc), which is believed to have apoptotic effects on host cells. Recombinant viruses with luciferase constructs are isolated and shown to stably maintain the Renilla luciferase gene and to express subgenomic mRNA encoding luciferase. SARS wt-Luc is a viable virus that allows studies of the effect of subgenomic manipulation on virus efficiacy, both in replication and subgenomic production. This approach offers an alternative to plaque assay analysis in testing the efficiency of anti-SARS agents
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
molecular biology
-
modification of the photoprotein aequorin by attaching selected fluorophores at a unique site on the protein. This will allow for in vitro transfer of bioluminescent energy from aequorin to the fluorophore thus creating an artificial jellyfish. The fluorophores are selected such that the excitation spectrum of the fluorophore overlaps with the emission spectrum of aequorin. By modifying aequorin with different fluorophores, bioluminescent labels with different emission maxima are produced, which will allow for the simultaneous detection of multiple analytes
molecular biology
Renilla sp.
-
Renilla luciferase, fused to biospecific sequences such as engineered antibodies, can be administered systemically to provide a novel, sensitive method for optical imaging based on expression of cell surface receptors in living organism
molecular biology
Renilla sp.
-
the development of variants of Renilla luciferase, which exhibit significantly improved properties compared with the native enzyme, will allow enhanced sensitivity in existing luciferase-based assays as well as enable the development of novel probes labeled with the luciferase protein
molecular biology
-
when aequorin is microinjected into cleavage-stage zebrafish embryos, it is largely used up by about 24 hours. Thus, it is not possible to image Ca2+ signals from later stages of zebrafish development using this approach. Transient expression of apoaequorin (i.e., the protein component of aequorin) using aeq-mRNA in zebrafish embryos and then reconstitution of intact aequorin in vivo by loading the coelenterazine cofactor into the embryos separately provides a valuable tool for monitoring Ca2+ signaling during the 2448 h post fertilization period of zebrafish development. Thus, it effectively extends the aequorin-based Ca2+-imaging window by an additional 24 hours
molecular biology
-
sensitive reproter for studies of gene expression, promoter activity, protein-protein interactions, signal transduction, tumor cell growth, response to therapy
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
pharmacology
Renilla sp.
-
investigations into regulation and functional roles of kinases
pharmacology
Renilla sp.
-
used as an assay for assessing potential liver toxicity by measuring GADD45-beta induction as an control for increased DNA damage
additional information
-
detection of tumor cells bearing a particular surface marker
additional information
-
Gluc reporter as a sensitive marker in elucidation endoplasmic reticulum stress in mammalian cells
additional information
-
imaging of T cells in the context of a competent immune system, bioluminescent imaging
additional information
-
monitor processing of proteins through the secretory pathway and endoplasmic reticulum
additional information
-
visualize proteins being secreted by exocytosis
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Cormier, M.J.; Hori, K.; Anderson, J.M.
Bioluminescence in coelenterates
Biochim. Biophys. Acta
346
137-164
1974
Renilla koellikeri, Renilla muelleri, Renilla reniformis
brenda
Matthews, J.C.; Hori, K.; Cormier, M.J.
Purification and properties of Renilla reniformis luciferase
Biochemistry
16
85-91
1977
Renilla reniformis
brenda
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
brenda
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
brenda
Matthews, J.C.; Hori, K.; Cormier, M.J.
Substrate and substrate analogue binding properties of Renilla luciferase
Biochemistry
16
5217-5220
1977
Renilla reniformis
brenda
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
brenda
Liu, J.; Escher, A.
Improved assay sensitivity of an engineered secreted Renilla luciferase
Gene
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153-159
1999
Renilla reniformis
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Liu, J.; O'Kane, D.J.; Escher, A.
Secretion of functional Renilla reniformis luciferase by mammalian cells
Gene
203
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1997
Renilla reniformis
brenda
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
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9
578-586
2004
Renilla reniformis
brenda
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
brenda
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
brenda
Roberts, R.; Yount, B.; Sims, A.; Baker, S.; Baric, R.
Renilla luciferase as a reporter to assess SARS-CoV mRNA transcription regulation and efficacy of anti-SARS-CoV agents
Adv. Exp. Med. Biol.
581
597-600
2006
Renilla sp.
brenda
Deo, S.K.; Mirasoli, M.; Daunert, S.
Bioluminescence resonance energy transfer from aequorin to a fluorophore: an artificial jellyfish for applications in multianalyte detection
Anal. Bioanal. Chem.
381
1387-1394
2005
Aequorea victoria
brenda
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
brenda
Inouye, S.; Tsuji, F.I.
Cloning and sequence analysis of cDNA for the Ca2+-activated photoprotein, clytin
FEBS Lett.
315
343-346
1993
Clytia gregaria
brenda
Inouye, S.
Blue fluorescent protein from the calcium-sensitive photoprotein aequorin is a heat resistant enzyme, catalyzing the oxidation of coelenterazine
FEBS Lett.
577
105-110
2004
Aequorea forskalea
brenda
Inouye, S.; Sasaki, S.
Blue fluorescent protein from the calcium-sensitive photoprotein aequorin: catalytic properties for the oxidation of coelenterazine as an oxygenase
FEBS Lett.
580
1977-1982
2006
Aequorea forskalea
brenda
Cheung, C.Y.; Webb, S.E.; Meng, A.; Miller, A.L.
Transient expression of apoaequorin in zebrafish embryos: extending the ability to image calcium transients during later stages of development
Int. J. Dev. Biol.
50
561-569
2006
Aequorea forskalea
brenda
Ohashi, W.; Inouye, S.; Yamazaki, T.; Hirota, H.
NMR analysis of the Mg2+-binding properties of aequorin, a Ca2+-binding photoprotein
J. Biochem.
138
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2005
Aequorea forskalea
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Tsuzuki, K.; Tricoire, L.; Courjean, O.; Gibelin, N.; Rossier, J.; Lambolez, B.
Thermostable mutants of the photoprotein aequorin obtained by in vitro evolution
J. Biol. Chem.
280
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2005
Aequorea victoria (Q6J4T7)
brenda
Tricoire, L.; Tsuzuki, K.; Courjean, O.; Gibelin, N.; Bourout, G.; Rossier, J.; Lambolez, B.
Calcium dependence of aequorin bioluminescence dissected by random mutagenesis
Proc. Natl. Acad. Sci. USA
103
9500-9505
2006
Aequorea victoria
brenda
Loening, A.M.; Fenn, T.D.; Wu, A.M.; Gambhir, S.S.
Consensus guided mutagenesis of Renilla luciferase yields enhanced stability and light output
Protein Eng. Des. Sel.
19
391-400
2006
Renilla sp.
brenda
Venisnik, K.M.; Olafsen, T.; Loening, A.M.; Iyer, M.; Gambhir, S.S.; Wu, A.M.
Bifunctional antibody-Renilla luciferase fusion protein for in vivo optical detection of tumors
Protein Eng. Des. Sel.
19
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2006
Renilla sp.
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Expression, purification and characterization of a photoprotein, clytin, from Clytia gregarium
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53
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Clytia gregaria
brenda
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All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin
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2005
Aequorea victoria (P07164)
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Hanson, J.; Reese, J.; Gorman, J.; Cash, J.; Fraizer, G.
Hormone treatment enhances WT1 activation of renilla luciferase constructs in LNCaP cells
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Renilla reniformis
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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
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Renilla reniformis
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Crystal structures of the luciferase and green fluorescent protein from Renilla reniformis
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Luciferase-YFP fusion tag with enhanced emission for single-cell luminescence imaging
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2007
Renilla reniformis
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Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase
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2008
Renilla muelleri (C9V492), Renilla muelleri
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Structure-function studies on the active site of the coelenterazine-dependent luciferase from Renilla
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RNA detection using peptide-inserted Renilla luciferase
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Renilla sp.
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Recombinant Gaussia luciferase: Overexpression, purification, and analytical application of a bioluminescent reporter for DNA hybridization
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Gaussia princeps (Q9BLZ2), Gaussia princeps
brenda
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Gaussia luciferase variant for high-throughput functional screening applications
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Gaussia princeps
brenda
Kaihara, A.; Umezawa, Y.; Furukawa, T.
Bioluminescent indicators for Ca2+ based on split renilla luciferase complementation in living cells
Anal. Sci.
24
1405-1408
2008
Renilla sp.
brenda
Inouye, S.; Sahara, Y.
Identification of two catalytic domains in a luciferase secreted by the copepod Gaussia princeps
Biochem. Biophys. Res. Commun.
365
96-101
2008
Gaussia princeps
brenda
Patel, K.; Ng, P.; Kuo, C.; Levy, S.; Levy, R.; Swartz, J.
Cell-free production of Gaussia princeps luciferase - antibody fragment bioconjugates for ex vivo detection of tumor cells
Biochem. Biophys. Res. Commun.
390
971-976
2009
Gaussia princeps
brenda
Cissell, K.A.; Rahimi, Y.; Shrestha, S.; Deo, S.K.
Reassembly of a bioluminescent protein renilla luciferase directed through DNA hybridization
Bioconjug. Chem.
20
15-19
2009
Renilla sp.
brenda
Suzuki, T.; Usuda, S.; Ichinose, H.; Inouye, S.
Real-time bioluminescence imaging of a protein secretory pathway in living mammalian cells using Gaussia luciferase
FEBS Lett.
581
4551-4556
2007
Gaussia princeps
brenda
Liu, X.; Kramer, J.A.; Hu, Y.; Schmidt, J.M.; Jiang, J.; Wilson, A.G.E.
Development of a high-throughput human hepG2 dual luciferase assay for detection of metabolically activated hepatotoxicants and genotoxicants
Int. J. Toxicol.
28
162-179
2009
Renilla sp.
brenda
Knappskog, S.; Ravneberg, H.; Gjerdrum, C.; Tre, C.; Stern, B.; Pryme, I.
The level of synthesis and secretion of Gaussia princeps luciferase in transfected CHO cells is heavily dependent on the choice of signal peptide
J. Biotechnol.
128
705-715
2007
Gaussia princeps (Q9BLZ2), Gaussia princeps
brenda
Ruecker, O.; Zillner, K.; Groebner-Ferreira, R.; Heitzer, M.
Gaussia-luciferase as a sensitive reporter gene for monitoring promoter activity in the nucleus of the green alga Chlamydomonas reinhardtii
Mol. Genet. Genomics
280
153-162
2008
Renilla sp., Gaussia princeps (Q9BLZ2), Gaussia princeps
brenda
Santos, E.B.; Yeh, R.; Lee, J.; Nikhamin, Y.; Punzalan, B.; Punzalan, B.; La Perle, K.; Larson, S.M.; Sadelain, M.; Brentjens, R.J.
Sensitive in vivo imaging of T cells using a membrane-bound Gaussia princeps luciferase
Nat. Med.
15
338-344
2009
Renilla sp., Gaussia princeps
brenda
Woo, J.; v. Arnim, A.G.
Mutational optimization of the coelenterazine-dependent luciferase from Renilla
Plant Methods
4
23
2008
Renilla reniformis
brenda
Herbst, K.J.; Allen, M.D.; Zhang, J.
The cAMP-dependent protein kinase inhibitor H-89 attenuates the bioluminescence signal produced by renilla luciferase
Plos One
4
e5642
2009
Renilla sp.
brenda
Badr, C.; Hewett, J.; Breakefield, X.; Tannous, B.
A highly sensitive assay for monitoring the secretory pathway and ER stress
PLoS ONE
6
e571
2007
Gaussia princeps
brenda
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
brenda
Stepanyuk, G.A.; Unch, J.; Malikova, N.P.; Markova, S.V.; Lee, J.; Vysotski, E.S.
Coelenterazine-v ligated to Ca2+-triggered coelenterazine-binding protein is a stable and efficient substrate of the red-shifted mutant of Renilla muelleri luciferase
Anal. Bioanal. Chem.
398
1809-1817
2010
Renilla muelleri (C9V492), Renilla muelleri
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
Gaussia, Oplophorus gracilirostris, Renilla reniformis
brenda
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
brenda
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)
brenda
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)
brenda
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)
-
brenda
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)
brenda
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)
brenda
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)
brenda
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
brenda
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)
brenda
Farkas, T.; Jaeaettelae, M.
Renilla luciferase-LC3 based reporter assay for measuring autophagic flux
Methods Enzymol.
588
1-13
2017
Renilla reniformis (P27652)
brenda
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)
brenda
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)
brenda
Broyles, D.B.; Dikici, E.; Daunert, S.; Deo, S.K.
Facile synthesis and characterization of a novel tamavidin-luciferase reporter fusion protein for universal signaling applications
Adv. Biosyst.
4
e1900166
2020
Gaussia princeps (Q9BLZ2)
brenda
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)
brenda
Larionova, M.; Markova, S.; Vysotski, E.
Bioluminescent and structural features of native folded Gaussia luciferase
J. Photochem. Photobiol. B
183
309-317
2018
Gaussia princeps (Q9BLZ2), Gaussia princeps
brenda
Zhang, C.; Cheng, L.; Dong, G.; Han, G.; Yang, X.; Tang, C.; Li, X.; Zhou, Y.; Du, L.; Li, M.
Novel photoactivatable substrates for Renilla luciferase imaging in vitro and in vivo
Org. Biomol. Chem.
16
4789-4792
2018
Renilla sp.
brenda
Ishibashi, M.; Kawanabe, R.; Amaba, N.; Arai, S.; Laksmi, F.; Komori, K.; Tokunaga, M.
Expression and characterization of the Renilla luciferase with the cumulative mutation
Protein Expr. Purif.
145
39-44
2018
Renilla reniformis (P27652), Renilla reniformis
brenda
Wu, N.; Kobayashi, N.; Tsuda, K.; Unzai, S.; Saotome, T.; Kuroda, Y.; Yamazaki, T.
Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR
Sci. Rep.
10
20069
2020
Gaussia princeps (Q9BLZ2)
brenda
Blower, I.; Tong, C.; Sun, X.; Murray, E.; Luckett, J.; Chan, W.; Williams, P.; Hill, P.
Gaussia luciferase as a reporter for quorum sensing in Staphylococcus aureus
Sensors
20
4305
2020
Gaussia princeps (Q9BLZ2)
brenda