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
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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 (Inhibitors
Inhibitors on EC 1.13.12.5 - Renilla-type luciferase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(2Z)-3-[[4-(dimethylamino)cyclohexa-1,5-dien-1-yl]amino]-1-phenylprop-2-en-1-one
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(3Z)-3-[[4-(dimethylamino)phenyl]methylidene]-1,3-dihydro-2H-indol-2-one
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common name SU4312
2-(4-ethoxyphenyl)-4-[(4-pyridin-2-ylpiperazin-1-yl)carbonyl]quinoline
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2-(4-methylphenyl)-4-[(4-pyrimidin-2-ylpiperazin-1-yl)carbonyl]quinoline
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2-hydroxy-N'-[(1E)-(2-hydroxyphenyl)methylidene]benzohydrazide
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common name SCS
4-(1,4-dioxa-8-azaspiro[4.5]dec-8-ylcarbonyl)-2-(4-ethoxyphenyl)quinoline
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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
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common name Evans Blue
4-[1-(1,3-benzothiazol-2-yl)-2-(4-methylpiperazin-1-yl)-2-oxoethyl]phenol
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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
ethyl 4-[[2-(4-ethoxyphenyl)quinolin-4-yl]carbonyl]piperazine-1-carboxylate
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glycerol
CAA01908.1
Renilla luciferase activity decreases at 0.8 and 1.2 M of glycerol through the obstruction of enzyme emitter site
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
N'-(3-chlorophenyl)-N-[(1Z)-(3-chlorophenyl)methylidene]imidoformamide
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common name DCB
N-benzyl-4-methylbenzenesulfonamide
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inhibition of purified enzyme, inducing activity in cell-based assay
thapsigargin
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0.03 microM, about 30% decrease of Gluc secretion and activity
dithiothreitol
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1 mM, complete inhibition of secretion for the first 3 h, secretion returned to normal level after 24 h
additional information
use of interleukin-2 and albumin signal peptide in vector leads to low levels of luciferase activity
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additional information
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use of interleukin-2 and albumin signal peptide in vector leads to low levels of luciferase activity
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additional information
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structure-activity relationship of luciferase inhibitors determined by quantitative high-throughput screening. Comparison of effect on various luciferase-based detection reagents
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additional information
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loss of enzymatic activity when in contact with substrate
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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
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additional information
Renilla sp.
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free oligonucleotide probe that competes to bind to the hybridizied probe-Rluc fragment complex inhibits the reassembly of Rluc, concentration-dependent; no activity of N-terminal or C-terminal Rluc fragments
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