1.13.12.5: Renilla-type luciferase
This is an abbreviated version!
For detailed information about Renilla-type luciferase, go to the full flat file.
Word Map on EC 1.13.12.5
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1.13.12.5
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bioluminescence
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luminescence
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photoproteins
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firefly
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agonist
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ventricular
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contractile
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tension
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ferret
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emit
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twitch
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isometric
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papillary
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depolarization
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ca2+-sensitive
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microinjected
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myocardium
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sarcoplasmic
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aequorea
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caffeine
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ryanodine
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myofilaments
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inotropic
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jellyfish
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calcium-sensitive
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luciferases
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victoria
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excitation-contraction
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fura-2
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replicons
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ca2+cyt
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tetanic
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light-emitting
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analysis
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glow
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trabeculae
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insp3
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biotechnology
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photinus
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signal-to-background
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ca2+-regulated
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ca2+-triggered
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barnacle
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luminometer
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luminescence-based
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myoplasmic
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ca2+-mobilizing
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molecular biology
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diagnostics
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pharmacology
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isovolumic
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charge-coupled
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luciferase-based
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pyralis
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photomultiplier
- 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
Reaction
Synonyms
19kOLase, aequorin, aequorin-1, BFP-aq, blue fluorescent protein from the calcium-binding photoprotein aequorin, Caussia princeps luciferase, clytin, extGLuc, extRLuc, firefly luciferase, fluc, Gaussia luciferase, Gaussia luciferase enzyme, Gaussia princeps luciferase, Gaussia-luciferase, GFP-aq, GLase, GLuc, Luc, luciferase, luciferase (Renilla luciferin), m-Rluc8, membrane-anchored RLUc, Oplophorus luciferase, PI-Rluc, R-Luc, Renilla luciferase, Renilla luciferase-547, Renilla luciferin 2-monooxygenase, Renilla muelleri luciferase, Renilla reniformis luciferase, Renilla-luciferase, Renilla-luciferin 2-monooxygenase, Renilla-type luciferase, RLase, RLase-547, RLuc, RLuc8, short peptide-inserted-Renilla luciferase
ECTree
1.13.12.5 Renilla-type luciferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.13.12.5 - Renilla-type luciferase
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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
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
-
-
-
?
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
-
-
-
-
?
bis-coelenterazine + O2
hnu + ?
-
assay at pH 7.6, about 100fold reduced relative luminescence
-
-
?
coelenterate-type luciferin + O2
oxidized coelenterate-type luciferin + CO2 + hv
-
-
-
-
?
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
-
?
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 + ?
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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
-
-
?
MeO-coelenterazine + O2
hnu + ?
-
assay at pH 7.6, about 100fold reduced relative luminescence
-
-
?
n-coelenterazine + O2
hnu + ?
-
assay at pH 7.6, about 100fold reduced relative luminescence
-
-
?
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: 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: 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: 49.5%
-
-
?
cf3-coelenterazine + O2
?
-
relative activity to native coelenterazine: 16.8%
-
-
?
cf3-coelenterazine + O2
?
-
relative activity to native coelenterazine: 5%
-
-
?
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 + 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
-
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 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)
-
-
?
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: 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: 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: 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: 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
-
-
-
-
?
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
-
-
?
