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(4S)-2-(6-hydroxy-1,3-benzoxazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2
?
-
decay time to 10%: 500 sec, relative specific activity: 13%
-
-
?
(4S)-2-(6-hydroxy-1-benzofuran-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2
?
-
decay time to 10%: 150 sec, relative specific activity: 1.7%
-
-
?
(4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2
?
-
decay time to 10%: 5700 sec, relative specific activity: 421%
-
-
?
(4S)-2-(6-hydroxy-1H-benzimidazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2
?
-
decay time to 10%: 400 sec, relative specific activity: 0.4%
-
-
?
(4S)-2-(6-hydroxy-1H-indol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid + ATP + O2
?
-
-
-
-
?
4'-methyl-D-luciferin + ATP + O2
?
-
-
-
?
5,5'-dimethylluciferin + ATP + O2
dehydroluciferin-adenylate + diphosphate
-
produces only red light, 6-amino and 4 hydroxy analogs tested
-
?
5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
5,5-dimethyloxyluciferin + hv
5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
5,5-dimethyloxyluciferin + hv + ?
-
-
-
-
?
5,5-dimethylluciferin + ATP
5,5-dimethyloxyluciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
5-methylluciferin + ATP
5-methyloxyluciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
5-methylluciferin + ATP + O2
?
-
-
-
?
5-monomethyl-luciferyl-O-adenosine monophosphate + ?
5-monomethyloxyluciferin + hv + ?
-
-
-
-
?
6'-amino-D-luciferin + ATP
? + hv
-
-
-
-
?
6'-amino-D-luciferin + ATP + O2
?
-
-
-
?
8-anilino-1-naphthalene-sulfonate + ?
?
-
-
-
?
adenosine 5'-tetraphosphate + Photinus luciferin
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
0.75% light response relative to ATP
-
?
ADP
ATP + AMP
-
-
reaction inhibited by P1,P5-di(adenosine-5'-)pentaphosphate, but independent of luciferin
?
arachidonic acid + ATP + CoA
arachidonoyl-CoA + ?
-
-
-
-
?
arachidonic acid + ATP + CoA
arachidonoyl-CoA + AMP + diphosphate
-
-
-
-
?
ATP + O2 + oxyluciferin
?
-
assay at pH 7.5, 24-27°C
-
-
?
coelenterazine disulfate + ATP + O2 + H2O
coelenteramide disulfate + AMP + CO2 + diphosphate
-
-
-
?
D-5,5-dimethylluciferyl-adenylate + O2
?
yellow-green color of luminescence
-
-
?
D-5,5-dimethylluciferyl-adenylate + O2 + ATP
?
red color of luminescence
-
-
?
D-aminoluciferin + ATP + O2
?
-
assay at 37°C. 5 min
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
D-luciferin + ATP
diphosphate + luciferyl-adenylate
-
-
-
r
D-luciferin + ATP + O2
luciferyl-adenylate + diphosphate
D-luciferin + ATP + O2
luciferyl-adenylate + diphosphate + H2O + hv
D-luciferin + ATP + O2
luciferyl-AMP + diphosphate
-
assay at pH 7.8
-
-
r
D-luciferin + ATP + O2
oxidized D-luciferin + AMP + CO2 + diphosphate
D-luciferin + ATP + O2
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
D-luciferin + ATP + O2
oxidized luciferin + AMP + CO2 + diphosphate
-
-
-
-
?
D-luciferin + ATP + O2
oxidized luciferin + AMP + CO2 + diphosphate + hv
D-luciferin + ATP + O2
oxyluciferin + CO2 + AMP + hv + diphosphate
-
-
-
-
?
D-luciferin + dATP + O2
?
-
-
-
-
?
D-luciferin + O2
?
-
10 microM, assay at pH 7.5
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
D-luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
D-luciferin + O2 + ATP
oxyluciferin + AMP + diphosphate + CO2 + light
-
-
-
?
D-luciferin + O2 + ATP
oxyluciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
r
D-luciferyl-adenylate + O2
oxyluciferin + CO2 + AMP + hv
-
-
-
ir
D-luciferyl-AMP + O2
dehydroluciferyl-AMP + H2O2
-
-
-
-
ir
D-luciferyl-O-adenosine monophosphate + ?
?
-
-
-
?
D-naphthylluciferin + ATP + O2
?
-
-
-
?
D-quinolylluciferin + ATP + O2
?
-
-
-
?
decanoic acid + ATP + CoA
decanoyl-CoA + AMP + diphosphate
dehydroluciferin + ATP
dehydroluciferyl-AMP + diphosphate
dehydroluciferin + ATP + O2
diphosphate + dehydroluciferin-adenylate
-
-
-
?
dehydroluciferin + CoA
dehydroluciferyl-CoA
-
-
-
-
?
dehydroluciferyladenylate + CoA
dehydroluciferyl-CoA + ?
-
-
-
-
?
deoxyATP + Photinus luciferin
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
fatty acid + ATP + CoA
fatty acyl-CoA + AMP
-
-
-
?
L-luciferin + CoA + ATP
luciferyl-CoA + AMP + diphosphate
-
L-luciferin is converted to luciferyl adenylate, and the adenyl group of luciferyl adenylate is then substituted to CoA-SH to give luciferyl-CoA. Even in presence of CoA-SH, D-luciferin is used for the light production reaction, but is not converted into luciferyl-CoA
-
-
?
lauric acid + ATP + CoA
lauroyl-CoA + AMP + diphosphate
linoleic acid + ATP + CoA
linoleoyl-CoA + AMP + diphosphate
linolenic acid + ATP + CoA
linolenoyl-CoA + AMP + diphosphate
luciferin + ATP + O2
?
-
assay at 25°C, pH 7.8
-
-
?
luciferin + ATP + O2
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
luciferin + ATP + O2
oxyluciferin + AMP + CO2 + diphosphate
-
-
-
-
?
luciferin + MgATP2-
AMP + diphosphate
luciferin + O2 + ATP
?
-
assay at pH 7.8
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
luciferin + O2 + ATP
oxyluciferin + AMP + diphosphate + CO2 + light
-
-
-
-
ir
luciferyl adenylate + O2
dehydroluciferyl adenylate + ?
-
-
-
-
?
luciferyl-adenylate
oxyluciferin + hnu
-
-
-
?
luciferyl-adenylate + O2
oxyluciferin + AMP + CO2 + hv
luciferyl-AMP + O2
oxyluciferin + hv + CO2 + AMP + diphosphate
-
-
-
-
r
luciferyl-O-adenosine monophosphate + ?
?
luciferyl-O-adenosine monophosphate + CoA
luciferyl-CoA + AMP
-
-
-
?
myristic acid + ATP + CoA
myristoyl-CoA + AMP + diphosphate
oleic acid + ATP + CoA
oleoyl-CoA + AMP + diphosphate
P1,P5-di(adenosine-5'-)pentaphosphate + Photinus luciferin
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
2.2% light response relative to ATP
-
?
palmitic acid + ATP + CoA
palmitoyl-CoA + AMP + diphosphate
-
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
Photinus luciferin + O2 + GTP
adenosine 5'-P1-tetraphospho-P4-5'''-guanosine
-
-
-
?
polyethylene glycol-6-amino-D-luciferin
? + hv
-
longer light emission
-
-
?
R-COOH + ATP
R-CO-AMP + diphosphate
additional information
?
-
5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
5,5-dimethyloxyluciferin + hv
-
-
-
-
?
5,5-dimethyl-luciferyl-O-adenosine monophosphate + ?
5,5-dimethyloxyluciferin + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
Amydetes vivianii
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
Amydetes vivianii
the enzyme display a typical change in bioluminescence color to red at acidic pH, high temperatures and in the presence of heavy metals
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
the larval fat body isozyme (AL2) displays very slow luminescence kinetics and a pH-insensitive spectrum. The adult lantern isozyme (AL1) displays flash-like kinetics and pH and metal sensitive bioluminescence spectra, and is at least 10 times catalytically more efficient than AL2
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
molecular dynamic is utilized to simulate free luciferase in explicit solvent at normal and at temperature above its Tm. The results of simulations are analyzed in order to evaluate the structural and dynamical properties of the enzyme
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
-
-
-
?
D-firefly luciferin + O2 + ATP
firefly oxyluciferin + CO2 + AMP + diphosphate + hv
the emission peak of this luciferase is 556 nm at pH 8.0, while it shifts to 606 nm at pH 6.0
-
-
?
D-luciferin + ATP + O2
?
-
-
-
-
?
D-luciferin + ATP + O2
?
-
assay at pH 7.5, 24-27°C
-
-
?
D-luciferin + ATP + O2
luciferyl-adenylate + diphosphate
-
-
-
r
D-luciferin + ATP + O2
luciferyl-adenylate + diphosphate
-
-
-
?
D-luciferin + ATP + O2
luciferyl-adenylate + diphosphate + H2O + hv
-
-
-
-
?
D-luciferin + ATP + O2
luciferyl-adenylate + diphosphate + H2O + hv
-
-
-
r
D-luciferin + ATP + O2
oxidized D-luciferin + AMP + CO2 + diphosphate
-
-
-
-
?
D-luciferin + ATP + O2
oxidized D-luciferin + AMP + CO2 + diphosphate
-
decay time to 10%: 23 sec, relative specific activity: 100%
-
-
?
D-luciferin + ATP + O2
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
assay at 25°C, pH 7.8
-
-
?
D-luciferin + ATP + O2
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + ATP + O2
oxidized luciferin + AMP + CO2 + diphosphate + hv
-
-
-
?
D-luciferin + ATP + O2
oxidized luciferin + AMP + CO2 + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
Macrolampis sp2
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
D-luciferin is (S)-2-[6'-hydroxy-2'-benzothiazolyl]-2-thiazoline-4-carboxylic acid (S)-2-[6-hydroxybenzothiazol-2-yl]-4,5-dihydrothiazole-4-carboxylic acid
-
-
r
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
D-luciferin is (S)-2-(6-hydroxy-2-benzothiazolyl)-2-thiazoline-4-carboxylic acid
the keto form of oxidized D-luciferin produces red light in chemiluminescence and yellow-green in bioluminescence
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized D-luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
D-luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
decanoic acid + ATP + CoA
decanoyl-CoA + AMP + diphosphate
-
-
-
?
decanoic acid + ATP + CoA
decanoyl-CoA + AMP + diphosphate
-
-
-
?
dehydroluciferin + ATP
dehydroluciferyl-AMP + diphosphate
-
-
-
r
dehydroluciferin + ATP
dehydroluciferyl-AMP + diphosphate
-
-
-
r
lauric acid + ATP + CoA
lauroyl-CoA + AMP + diphosphate
-
-
-
?
lauric acid + ATP + CoA
lauroyl-CoA + AMP + diphosphate
-
-
-
?
linoleic acid + ATP + CoA
linoleoyl-CoA + AMP + diphosphate
-
-
-
-
?
linoleic acid + ATP + CoA
linoleoyl-CoA + AMP + diphosphate
-
-
-
-
?
linoleic acid + ATP + CoA
linoleoyl-CoA + AMP + diphosphate
linoleic acid concentration above 10 microM has an inhibitory effect
-
-
?
linolenic acid + ATP + CoA
linolenoyl-CoA + AMP + diphosphate
-
-
-
-
?
linolenic acid + ATP + CoA
linolenoyl-CoA + AMP + diphosphate
-
-
-
-
?
luciferin + ATP + O2
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
luciferin + ATP + O2
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
luciferin + ATP + O2
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
r
luciferin + MgATP2-
AMP + diphosphate
-
-
-
?
luciferin + MgATP2-
AMP + diphosphate
-
-
-
-
?
luciferin + MgATP2-
AMP + diphosphate
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
luciferase modulates emission color by controlling the resonance-based delocalization of the anionic keto form of the oxyluciferin excited state
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
luciferase modulates emission color by controlling the resonance-based deloclization of the anionic keto form of the oxyluciferin excited state
-
?
luciferyl-adenylate + O2
oxyluciferin + AMP + CO2 + hv
-
-
-
ir
luciferyl-adenylate + O2
oxyluciferin + AMP + CO2 + hv
-
-
-
ir
luciferyl-O-adenosine monophosphate + ?
?
-
-
-
-
?
luciferyl-O-adenosine monophosphate + ?
?
-
-
-
-
?
myristic acid + ATP + CoA
myristoyl-CoA + AMP + diphosphate
-
-
-
?
myristic acid + ATP + CoA
myristoyl-CoA + AMP + diphosphate
-
-
-
?
oleic acid + ATP + CoA
oleoyl-CoA + AMP + diphosphate
-
-
-
-
?
oleic acid + ATP + CoA
oleoyl-CoA + AMP + diphosphate
-
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
highly specific for ATP
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
enzyme produced in Sf9 cells requires less luciferin than mammalian or plant cells
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the true substrate is MgATP2-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the true substrate is MgATP2-
-
?
Photinus luciferin + O2 + ATP
oxidized Photinus luciferin + CO2 + H2O + AMP + diphosphate + hv
-
the true substrate is MgATP2-
-
?
R-COOH + ATP
R-CO-AMP + diphosphate
-
-
-
r
R-COOH + ATP
R-CO-AMP + diphosphate
-
-
-
r
additional information
?
-
no fatty acyl-CoA synthetase activity with octanoic acid and palmitic acid
-
-
?
additional information
?
-
-
12 nucleoside triphosphates examined
-
-
?
additional information
?
-
no fatty acyl-CoA synthetase activity with octanoic acid and palmitic acid
-
-
?
additional information
?
-
analysis of reaction parameters, detailed overview
-
-
?
additional information
?
-
-
analysis of reaction parameters, detailed overview
-
-
?
additional information
?
-
analysis of reaction parameters, detailed overview
-
-
?
additional information
?
-
-
analysis of reaction parameters, detailed overview
-
-
?
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(2E)-1-(1-benzofuran-2-yl)-3-(4-methylphenyl)prop-2-en-1-one
-
-
(2E)-1-(1-benzofuran-2-yl)-3-phenylprop-2-en-1-one
-
-
(2E)-1-(2-hydroxyphenyl)-3-(4-methylphenyl)prop-2-en-1-one
-
-
(2E)-1-(5-chlorothiophen-2-yl)-3-(4-methylphenyl)prop-2-en-1-one
-
-
(2E)-1-(5-chlorothiophen-2-yl)-3-phenylprop-2-en-1-one
-
-
(2E)-2-benzylidene-3,4-dihydronaphthalen-1(2H)-one
-
(2E)-2-[(2-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(2-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(2-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(2-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(2-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(3-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(3-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(3-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(3-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(3-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(4-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(4-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(4-ethoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(4-ethylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(4-fluorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(4-hydroxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(4-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(4-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[(pyridin-3-yl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[[4-(benzyloxy)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[[4-(diethylamino)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-6-methoxy-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-7-methoxy-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-8-methoxy-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[[4-(methylsulfanyl)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-2-[[4-(trifluoromethyl)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-5-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-6-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-7-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2E)-8-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
-
(2R)-2-[4-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)phenyl]propanoic acid
common name indoprofen
(2Z)-1-(4-chlorophenyl)-3-(pyridin-2-ylamino)prop-2-en-1-one
-
(2Z)-3-[(2-bromophenyl)amino]-1-pyridin-2-ylprop-2-en-1-one
-
(2Z)-3-[(4-fluorophenyl)amino]-1-furan-2-ylprop-2-en-1-one
-
(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
(6E)-6-[(3-carboxy-4-hydroxyphenyl)methylidene]-5-oxo-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
-
-
(7E)-7-[(4-methylphenyl)methylidene]-8-oxo-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
-
-
1-phenyl-3-(5-phenylpyridin-2-yl)urea
-
10 microM, 20% inhibition
1-[3-(6-ethoxy-1,3-benzothiazol-2-yl)thiophen-2-yl]urea
-
2,4-dimethoxy-N-(5-methylpyridin-2-yl)benzamide
2-(2-amino-3-methoxyphenyl)-4H-chromen-4-one
common name PD98059
2-(2-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole
2-(2-imino-4,5,6,7-tetrahydro-1,3-benzothiazol-3(2H)-yl)-1-(4-methylphenyl)ethanone
common name pifithrin-alpha
2-(2-methoxyphenyl)-1,3-benzothiazole
2-(3,4-dimethoxyphenyl)-1,3-benzothiazole
2-(3,4-dimethoxyphenyl)-6-methoxy-1,3-benzothiazole
2-(3-fluorophenyl)-1,3-benzothiazole
2-(3-fluorophenyl)-6-methoxy-1,3-benzothiazole
2-(4-chlorophenyl)-1,3-benzothiazole
2-(4-chlorophenyl)-6-methoxy-1,3-benzothiazole
2-(4-ethoxyphenyl)-4-[(4-methylpiperazin-1-yl)carbonyl]quinoline
-
2-(4-ethoxyphenyl)-4-[(4-pyridin-2-ylpiperazin-1-yl)carbonyl]quinoline
-
2-(4-fluorophenyl)-6-methoxy-1,3-benzothiazole
2-(4-methoxyphenyl)-1,3-benzothiazole
2-(4-methylphenyl)-4-[(4-pyrimidin-2-ylpiperazin-1-yl)carbonyl]quinoline
-
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
2-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
2-(5-naphthalen-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
2-(5-pyridin-4-yl-1,2,4-oxadiazol-3-yl)pyridine
2-(6'-hydroxy-2'-benzothiazolyl)-4-hydroxymethylthiazole
-
competitive inhibitor
2-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
2-benzylidene-1H-indene-1,3(2H)-dione
-
-
2-hydroxy-5-[(E)-(1-oxo-3,4-dihydronaphthalen-2(1H)-ylidene)methyl]benzoic acid
-
-
2-hydroxy-N'-[(1E)-(2-hydroxyphenyl)methylidene]benzohydrazide
common name SCS
2-methyl-6-(phenylethynyl)pyridine
common name MPEB
2-methyl-6-[(Z)-2-phenylethenyl]pyridine
common name SIB1893
2-[(4-methylphenyl)methylidene]-1H-indene-1,3(2H)-dione
-
-
2-[(4-methylphenyl)methyl]-3,4-dihydronaphthalen-1(2H)-one
-
-
2-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]pyridine
2-[5-(3,4-dichlorophenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
2-[5-(3-chloro-4-methylphenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
2-[5-(3-chlorophenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
2-[5-(5-bromofuran-2-yl)-1,2,4-oxadiazol-3-yl]pyridine
-
2-[[4-(dimethylamino)phenyl]methyl]-3,4-dihydronaphthalen-1(2H)-one
-
-
3,4-dichloro-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 13% inhibition
3,4-dimethoxy-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 26% inhibition
-
3,5-diphenyl-1,2,4-oxadiazole
-
-
3-(2-hydroxyphenyl)-1H-benzo[f]chromen-1-one
common name flavonoid
3-(2-methoxyphenyl)-5-phenyl-1,2,4-oxadiazole
3-(4-methylphenyl)-4,5-dihydro-2H-benzo[g]indazole
-
-
3-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
3-chloro-N-(5-phenylpyridin-2-yl)benzamide
-
-
3-methyl-2-[(E)-phenyldiazenyl]phenol
3-pyridin-2-yl-1,2,4-oxadiazol-5-yl biphenyl-4-carboxylate
3-[5-(2-fluorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
3-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
3-[5-(3-chlorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
3-[5-(3-methoxyphenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
3-[5-(4-chlorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
3-[5-[2-(trifluoromethyl)phenyl]-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
3-[5-[4-(trifluoromethyl)phenyl]-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
4-((7-[4-(trifluoromethyl)benzyl]-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy)aniline
-
7% inhibition
4-(1,3-benzothiazol-2-yl)-N,N-dimethylaniline
4-(1,3-benzothiazol-2-yl)benzonitrile
4-(1,4-dioxa-8-azaspiro[4.5]dec-8-ylcarbonyl)-2-(4-ethoxyphenyl)quinoline
-
4-(1-methylethoxy)-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 12% inhibition
-
4-(4-aminophenoxy)-7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-2-amine
-
-
4-(4-methylphenyl)-5,6-dihydrobenzo[h]quinazolin-2-amine
-
-
4-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
4-(6-methoxy-1,3-benzothiazol-2-yl)-N,N-dimethylaniline
4-(6-methoxy-1,3-benzothiazol-2-yl)benzonitrile
4-(7H-pyrrolo[2,3-d]pyrimidin-4-yloxy)aniline
-
19% inhibition
4-(dimethylamino)-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 35% inhibition
4-([2-(methylsulfanyl)-7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
31% inhibition
4-([2-(methylsulfonyl)-7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
9% inhibition
4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)-N,N-dimethylaniline
-
-
4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)-N-methylaniline
-
-
4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
4-([7-(2-methylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
4-([7-(3-methylbut-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
4-([7-(3-methylbutyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
4-([7-(4-methoxybenzyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
26% inhibition
4-([7-(prop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
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-amino-N-(5-phenylpyridin-2-yl)benzamide
-
-
4-chloro-N-(5-phenylpyridin-2-yl)benzamide
-
-
4-methoxy-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 28% inhibition
4-methoxy-N-[(4-methylpyridin-2-yl)carbamoyl]benzamide
-
4-methyl-N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 18% inhibition
4-methyl-N-(phenylmethyl)benzenesulfonamide
-
-
4-[(7-benzyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline
-
46% inhibition
4-[(7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline
-
-
4-[(7-ethenyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline
-
-
4-[(7-ethyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline
-
-
4-[(7-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline
-
48% inhibition
4-[1-(1,3-benzothiazol-2-yl)-2-(4-methylpiperazin-1-yl)-2-oxoethyl]phenol
-
4-[3-(2-methoxyphenyl)-1,2,4-oxadiazol-5-yl]pyridine
4-[5-(2-chlorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
4-[5-(2-fluorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
4-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]-N,N-dimethylaniline
4-[5-(3-chlorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
4-[5-(3-fluorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
-
5'-O-[(N-dehydroluciferyl)-sulfamoyl]-adenosine
-
stable and potent reversibel inhibitor
5'-O-[N-(dehydroluciferyl)sulfamoyl]adenosine
competitive inhibitor
5'-O-[[2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazole-4-carbonyl]sulfamoyl]adenosine
non-competitive inhibitor
-
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
5-(2-bromophenyl)-3-(4-methylphenyl)-1,2,4-oxadiazole
-
5-(2-chloro-4-methylphenyl)-3-phenyl-1,2,4-oxadiazole
-
5-(2-fluorophenyl)-3-(4-methoxyphenyl)-1,2,4-oxadiazole
5-(4-fluorophenyl)-3-(3-methylphenyl)-1,2,4-oxadiazole
5-(ethanesulfonyl)-2-(naphthalen-2-yl)-1,3-benzoxazole
non-competitive inhibitor
-
5-anilino-1-naphthalene sulfonate
5-methyl-N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide
-
5-naphthalen-2-yl-3-phenyl-1,2,4-oxadiazole
-
5-[(2E)-4-(4-bromophenyl)-4-oxobut-2-en-1-yl]-2-hydroxybenzoic acid
luciferin competitor
-
5-[(E)-(6-bromo-1-oxo-3,4-dihydronaphthalen-2(1H)-ylidene)methyl]-2-hydroxybenzoic acid
-
-
6-methoxy-2-(2-methoxyphenyl)-1,3-benzothiazole
6-methoxy-2-(3-methylphenyl)-1,3-benzothiazole
6-methoxy-2-(4-methoxyphenyl)-1,3-benzothiazole
6-methoxy-2-[2-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
6-methoxy-2-[3-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
6-methyl-2-[(Z)-phenyldiazenyl]pyridin-3-ol
common name SIB1757
6-toluidino-2-naphthalene sulfonate
arachidonic acid
concentration above 10 microM
bovine serum albumin
-
inhibition when present in large excess
-
butanoic acid
-
IC50: 13.6 mM
CoA
-
above 0.1 mM, N-terminal domain
D-luciferin
-
inhibits CoA-ligase activity with L-luciferin, IC50: 0.135 mM against 0.1 mM L-luciferin
Decanoic acid
-
IC50: 0.0132 mM
dehydroluciferyl adenylate
dehydroluciferyl-adenylate
-
tight-binding competitive inhibitor
dehydroluciferyl-CoA
-
IC50: 0.005 mM
Dodecanol
-
mixed-type inhibitor
dodecylamine
-
noncompetitive inhibitor
ethyl 4-[[2-(4-ethoxyphenyl)quinolin-4-yl]carbonyl]piperazine-1-carboxylate
-
ethyl [4-(4-aminophenoxy)-7H-pyrrolo[2,3-d]pyrimidin-7-yl]acetate
-
33% inhibition
ethyl-2-benzothiazole sulfonate
-
competitive inhibitor
geneticin
-
induces nonsense suppression
gentamicin
-
induces nonsense suppression
Halothane
non-competitive inhibitor
hexadecanoic acid
-
IC50: 0.00067 mM
hexanoic acid
-
IC50: 3.4 mM
L-1-tosylamido-2-phenethyl chlorometyl ketone
-
competitive inhibitor with respect to luciferin, noncompetitive with respect to ATP
L-AMP
a potent luciferase inhibitor
Limulus amebocyte lysate
-
decreased luminescence intensity to 10%
-
linoleic acid
concentration above 10 microM
N'-(3-chlorophenyl)-N-[(1Z)-(3-chlorophenyl)methylidene]imidoformamide
common name DCB
N,N-dimethyl-4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
N,N-dimethyl-4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
N-(4-ethoxyphenyl)-2-methoxybenzamide
-
N-(5-methylpyridin-2-yl)benzamide
-
-
N-(5-phenylpyridin-2-yl)benzamide
-
10 microM, 27% inhibition
N-(5-phenylpyridin-2-yl)butanamide
-
10 mciroM, 22% inhibition
N-(5-phenylpyridin-2-yl)cyclohexanecarboxamide
-
-
N-(6-ethoxy-1,3-benzothiazol-2-yl)-2-methylfuran-3-carboxamide
-
N-(6-methoxy-1,3-benzothiazol-2-yl)-2-methylfuran-3-carboxamide
-
N-(6-methoxy-1,3-benzothiazol-2-yl)-3-methylthiophene-2-carboxamide
-
-
N-(6-methyl-1,3-benzothiazol-2-yl)thiophene-2-carboxamide
N-(6-phenylpyridin-2-yl)benzamide
-
10 microM, 30% inhibition
N-benzyl-5-phenylpyridin-2-amine
-
10 microM, 20% inhibition
N-methyl-4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
N-methyl-4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
-
-
N-pyridin-2-ylbenzamide
-
N-quinolin-2-ylbenzamide
-
-
N-tosyl-L-lysine chloromethyl ketone
-
-
N-tosyl-L-phenylalanine chloromethyl ketone
N-[3-(6-methoxy-1,3-benzothiazol-2-yl)phenyl]acetamide
N-[4-(1,3-benzothiazol-2-yl)phenyl]acetamide
N-[5-(3,4-dichlorophenyl)pyridin-2-yl]benzamide
-
10 microM, 4% inhibition
N-[5-(3-chlorophenyl)pyridin-2-yl]benzamide
-
10 microM, 38% inhibition
N-[5-(4-chlorophenyl)pyridin-2-yl]benzamide
-
-
N-[5-(4-methoxyphenyl)pyridin-2-yl]benzamide
-
-
N-[5-(4-methylphenyl)pyridin-2-yl]benzamide
-
10 microM, 51% inhibition
N-[5-(4-tert-butylphenyl)pyridin-2-yl]benzamide
-
10 microM, 49% inhibition
N-[5-[(2,2-dimethylpropanoyl)amino]pyridin-2-yl]-3-hydroxybenzamide
-
N-[5-[4-(1-methylethoxy)phenyl]pyridin-2-yl]benzamide
-
10 microM, 38% inhibition
N-[5-[4-(dimethylamino)phenyl]pyridin-2-yl]benzamide
-
10 microM, 14% inhibition
N-[5-[4-(trifluoromethyl)phenyl]pyridin-2-yl]benzamide
-
10 microM, 39% inhibition
N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide
-
NFkappaBAI4
non-competitive inhibitor
-
octadecanoic acid
-
IC50: 0.00063 mM
octanoic acid
-
IC50: 2.9 mM
oleic acid
concentration above 10 microM
phenyl (5-phenylpyridin-2-yl)carbamate
-
-
-
pifithrin-alpha
20 microM, above 95% inhibition
SMT C1100
non-competitive inhibitor, utrophin modulator, phase II clinical compound SMT C1100 for the treatment of Duchenne muscular dystrophy
-
tetradecanoic acid
-
IC50: 0.00068 mM
[2-(4-ethoxyphenyl)quinolin-4-yl][4-(pyridin-2-yl)piperazin-1-yl]methanone
ATP competitor
-
[4-(6-methoxynaphthalen-2-yl)phenyl]acetic acid
luciferin competitor
-
2,4-dimethoxy-N-(5-methylpyridin-2-yl)benzamide
-
-
2,4-dimethoxy-N-(5-methylpyridin-2-yl)benzamide
-
2,4-dimethoxy-N-(5-methylpyridin-2-yl)benzamide
non-competitive inhibitor
2-(2-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
-
-
2-(2-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
-
-
2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole
luciferin competitor
2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(2-methoxyphenyl)-1,3-benzothiazole
-
-
2-(2-methoxyphenyl)-1,3-benzothiazole
-
-
2-(3,4-dimethoxyphenyl)-1,3-benzothiazole
-
-
2-(3,4-dimethoxyphenyl)-1,3-benzothiazole
-
-
2-(3,4-dimethoxyphenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(3,4-dimethoxyphenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(3-fluorophenyl)-1,3-benzothiazole
-
-
2-(3-fluorophenyl)-1,3-benzothiazole
-
-
2-(3-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(3-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(4-chlorophenyl)-1,3-benzothiazole
-
-
2-(4-chlorophenyl)-1,3-benzothiazole
-
-
2-(4-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(4-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(4-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(4-fluorophenyl)-6-methoxy-1,3-benzothiazole
-
-
2-(4-methoxyphenyl)-1,3-benzothiazole
-
-
2-(4-methoxyphenyl)-1,3-benzothiazole
-
-
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
2-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
2-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
2-(5-pyridin-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
2-(5-pyridin-4-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
2-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
2-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]pyridine
-
-
3',5'-cyclic AMP
-
competitive inhibitor
3-(2-methoxyphenyl)-5-phenyl-1,2,4-oxadiazole
-
-
3-(2-methoxyphenyl)-5-phenyl-1,2,4-oxadiazole
-
-
3-methyl-2-[(E)-phenyldiazenyl]phenol
-
-
3-methyl-2-[(E)-phenyldiazenyl]phenol
-
-
3-pyridin-2-yl-1,2,4-oxadiazol-5-yl biphenyl-4-carboxylate
-
-
3-pyridin-2-yl-1,2,4-oxadiazol-5-yl biphenyl-4-carboxylate
-
-
3-[5-(2-fluorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
decrease of Fluc proteolysis, 2 microM
3-[5-(2-fluorophenyl)-1,2,4-oxadiazol-3-yl]benzoic acid
-
4-(1,3-benzothiazol-2-yl)-N,N-dimethylaniline
-
-
4-(1,3-benzothiazol-2-yl)-N,N-dimethylaniline
-
-
4-(1,3-benzothiazol-2-yl)benzonitrile
-
-
4-(1,3-benzothiazol-2-yl)benzonitrile
-
-
4-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
4-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
-
-
4-(6-methoxy-1,3-benzothiazol-2-yl)-N,N-dimethylaniline
-
-
4-(6-methoxy-1,3-benzothiazol-2-yl)-N,N-dimethylaniline
-
-
4-(6-methoxy-1,3-benzothiazol-2-yl)benzonitrile
-
-
4-(6-methoxy-1,3-benzothiazol-2-yl)benzonitrile
-
-
4-[3-(2-methoxyphenyl)-1,2,4-oxadiazol-5-yl]pyridine
-
-
4-[3-(2-methoxyphenyl)-1,2,4-oxadiazol-5-yl]pyridine
-
-
4-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]-N,N-dimethylaniline
-
-
4-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]-N,N-dimethylaniline
-
-
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
-
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
-
-
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
-
-
5-(2-fluorophenyl)-3-(4-methoxyphenyl)-1,2,4-oxadiazole
-
-
5-(2-fluorophenyl)-3-(4-methoxyphenyl)-1,2,4-oxadiazole
-
-
5-(4-fluorophenyl)-3-(3-methylphenyl)-1,2,4-oxadiazole
-
-
5-(4-fluorophenyl)-3-(3-methylphenyl)-1,2,4-oxadiazole
-
-
5-anilino-1-naphthalene sulfonate
-
-
5-anilino-1-naphthalene sulfonate
-
competitive inhibitor
6-methoxy-2-(2-methoxyphenyl)-1,3-benzothiazole
-
-
6-methoxy-2-(2-methoxyphenyl)-1,3-benzothiazole
-
-
6-methoxy-2-(3-methylphenyl)-1,3-benzothiazole
-
-
6-methoxy-2-(3-methylphenyl)-1,3-benzothiazole
-
-
6-methoxy-2-(4-methoxyphenyl)-1,3-benzothiazole
-
-
6-methoxy-2-(4-methoxyphenyl)-1,3-benzothiazole
-
-
6-methoxy-2-[2-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
-
-
6-methoxy-2-[2-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
-
-
6-methoxy-2-[3-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
-
-
6-methoxy-2-[3-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
-
-
6-toluidino-2-naphthalene sulfonate
-
-
6-toluidino-2-naphthalene sulfonate
-
competitive inhibitor
arsenate
-
lowers the flash height and extends the light emission for a given amount of ATP
arsenate
-
reversible inhibition
arsenate
-
lowers the flash height and extends the light emission for a given amount of ATP
ATP
-
-
ATP
-
uncomplexed ATP is a competitive inhibitor with respect to MgATP2- complex
ATP
-
noncompetitive inhibitor
ATP
-
uncomplexed ATP is a competitive inhibitor with respect to MgATP2- complex
dehydroluciferin
-
dehydroluciferin
-
competitive inhibitor
dehydroluciferyl adenylate
-
dehydroluciferyl adenylate
-
IC50: 6 nM
dehydroluciferyl adenylate
-
diphosphate
-
-
diphosphate
depending on conditions
dodecanoic acid
-
IC50: 0.0012 mM
dodecanoic acid
-
competitive
L-luciferin
-
Luciferin
-
-
Luciferin
-
noncompetitive inhibitor
Luciferin
-
inhibition if concentration is higher than 0.05 mM
N-(6-methyl-1,3-benzothiazol-2-yl)thiophene-2-carboxamide
-
N-(6-methyl-1,3-benzothiazol-2-yl)thiophene-2-carboxamide
-
-
N-tosyl-L-phenylalanine chloromethyl ketone
-
-
N-tosyl-L-phenylalanine chloromethyl ketone
-
competitive inhibitor with respect to luciferin, noncompetitive with respect to ATP, pH dependent, enzyme protected by dehydroluciferin-AMP
N-[3-(6-methoxy-1,3-benzothiazol-2-yl)phenyl]acetamide
-
-
N-[3-(6-methoxy-1,3-benzothiazol-2-yl)phenyl]acetamide
-
-
N-[4-(1,3-benzothiazol-2-yl)phenyl]acetamide
-
-
N-[4-(1,3-benzothiazol-2-yl)phenyl]acetamide
-
-
oxyluciferin
-
oxyluciferin
-
competitive inhibitor
Procion blue MX-R
-
irreversible inhibitor, enzyme protected by luciferin, ATP and MgATP2-
Procion blue MX-R
-
irreversible inhibitor, enzyme protected by luciferin, ATP and MgATP2-; time dependent
resveratrol
-
resveratrol is 3,5,4'-trihydroxystilbene, potent inhibitor
resveratrol
non-competitive inhibitor
additional information
-
binding of one of the substrates ATP or luciferin to luciferase decreases the affinity of the enzyme to the other substrate
-
additional information
irreversible aggregation because of the exposure of its hydrophobic sites followed by structural changes leads to its further inactivation
-
additional information
-
irreversible aggregation because of the exposure of its hydrophobic sites followed by structural changes leads to its further inactivation
-
additional information
the extensive applications of Firefly luciferase in numerous biological, biomedical, and clinical investigations renders an urgent need for efficient and biocompatible Fluc inhibitors for the construction of novel assay platforms
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.176
(4S)-2-(6-hydroxy-1,3-benzoxazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.07
(4S)-2-(6-hydroxy-1-benzofuran-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.061
(4S)-2-(6-hydroxy-1-benzothiophen-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 9.1, temperature not specified in the publication
0.02
(4S)-2-(6-hydroxy-1H-benzimidazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid
-
pH 8.5, temperature not specified in the publication
0.00025 - 0.0008
5,5-dimethyl-luciferyl-O-adenosine monophosphate
0.00076 - 25
D-firefly luciferin
0.00038 - 0.0126
D-luciferyl-O-adenosine monophosphate
0.0149
dehydroluciferyl-adenylate
-
-
0.00741 - 0.0163
lauric acid
0.0136
linolenic acid
-
-
0.0006 - 0.0127
luciferyl-O-adenosine monophosphate
additional information
additional information
-
0.00025
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, wild-type enzyme
0.0003
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme F250S
0.0003
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme G246A
0.0003
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, wild-type enzyme
0.0004
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme A243G
0.0008
5,5-dimethyl-luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme S247F
0.00015
ATP
-
-
0.00015
ATP
-
immobilized on activated Sepharose
0.001
ATP
mutant enzyme I423L/D436G/L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.002
ATP
-
immobilized enzyme
0.003
ATP
-
150 microM luciferin, two-site binding model
0.0038
ATP
-
150 microM luciferin, presence of 1 microM of N-quinolin-2-ylbenzamide, two-site binding model
0.004
ATP
free enzyme, in 0.02 M Tris-acetate buffer, pH 7.8, containing 12 mM magnesium acetate, 0.2 mM EDTA, and 0.3 mM dithiothreitol
0.004
ATP
-
pH 8.0, temperature not specified in the publication, isoenzyme AL1
0.005
ATP
Amydetes vivianii
pH 8.0, 22°C, mutant enzyme E270A
0.007
ATP
-
pH 8.0, temperature not specified in the publication, isoenzyme AL2
0.008
ATP
mutant I423L/D436G/L530R, in the presence of 0.001 mM D-luciferin
0.009
ATP
Amydetes vivianii
pH 8.0, 22°C, wild-type enzyme
0.009
ATP
mutant enzyme D436G, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.009
ATP
mutant enzyme D436G, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.009
ATP
mutant D436G, in the presence of 0.001 mM D-luciferin
0.017
ATP
Amydetes vivianii
pH 8.0, 22°C, mutant enzyme E270G
0.029
ATP
recombinant mutant enzyme G246A, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.04
ATP
mutant E354K/ins356K
0.04
ATP
pH 7.8, temperature not specified in the publication, mutant enzyme H489M
0.041
ATP
recombinant mutant enzyme V241I/G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.0456
ATP
mutant enzyme I432L, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.047
ATP
mutant enzyme I423L, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.047
ATP
mutant I423L, in the presence of 0.001 mM D-luciferin
0.0485
ATP
-
addition of luciferin 30 min after ATP
0.05
ATP
pH 7.8, 25°C, wild-type enzyme
0.05
ATP
mutant E354Q/ins356K
0.05
ATP
pH 7.8, 25°C, mutant enzyme R330Q
0.0538
ATP
mutant enzyme L530R, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.054
ATP
mutant enzyme L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.054
ATP
mutant L530R, in the presence of 0.001 mM D-luciferin
0.0594
ATP
-
addition of luciferin 30 min before ATP
0.06
ATP
-
adenylate kinase activity
0.06
ATP
recombinant mutant enzyme G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.06
ATP
recombinant mutant enzyme G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.06
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][acetate]
0.06
ATP
pH 7.8, temperature not specified in the publication, mutant enzyme H489K
0.06
ATP
pH 7.8, temperature not specified in the publication, wild-type enzyme
0.061
ATP
recombinant mutant enzyme G246A/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.071
ATP
wild-type luciferase
0.075
ATP
pH 7.8, 25°C, mutant enzyme K329I
0.077
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][acetate]
0.0778
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][lactate]
0.0778
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][propionate]
0.08
ATP
pH 7.8, 22°C, recombinant mutant Y255F
0.086
ATP
-
0.094 mM luciferin, in presence of alpha-synuclein
0.086
ATP
pH 7.8, 22°C, recombinant wild-type enzyme
0.09
ATP
pH 7.8, temperature not specified in the publication, mutant enzyme H489D
0.093
ATP
recombinant mutant enzyme V241I/G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.094
ATP
-
150 microM luciferin, presence of 1 microM of N-quinolin-2-ylbenzamide, two-site binding model
0.095
ATP
mutant E354R/ins356K
0.0955
ATP
in 50 mM Tricine-NaOH buffer with 10 mM MgSO4, at pH 7.8
0.1
ATP
-
35°C, pH 8.5, mutant A296C/A326C
0.1
ATP
-
mutant D476N, pH 7, 25°C
0.1
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
0.1
ATP
-
wild-type, pH 8, 25°C
0.1
ATP
pH 7.8, temperature not specified in the publication, mutant enzyme H461D
0.1 - 1
ATP
-
pH 7.8, temperature not specified in the publication, native enzyme
0.11
ATP
-
soluble and immobilized enzyme
0.11
ATP
-
two catalytically active sites: first site with a Km for ATP of 0.11 mM is responsible for initial flash, a second site with a Km for ATP of 0.02 mM catalyses the continuous low production of light
0.111
ATP
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
0.111
ATP
-
pH 7.8, temperature not specified in the publication, native enzyme
0.1125
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][lactate]
0.114
ATP
-
0.094 mM luciferin, without alpha-synuclein
0.114
ATP
-
0.188 mM luciferin, in presence of alpha-synuclein
0.12
ATP
wild-type luciferase
0.125
ATP
-
tricine buffer
0.125
ATP
-
25°C, pH 8, wild-type
0.126
ATP
pH 7.8, 22°C, recombinant mutant R213K/T214N
0.133
ATP
recombinant mutant enzyme F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.133
ATP
-
wild-type luciferase
0.135
ATP
wild-type luciferase
0.135
ATP
pH 7.8, 22°C, recombinant wild-type enzyme
0.138
ATP
-
150 microM luciferin, two-site binding model
0.14
ATP
at pH 7.8, in 50 mM Tricine-NaOH buffer with 10 mM MgSO4
0.15
ATP
-
mutant D474K, pH 8.5, 25°C
0.151
ATP
recombinant mutant enzyme V241I/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.154
ATP
pH 7.5, temperature not specified in the publication
0.157
ATP
-
0.188 mM luciferin, without alpha-synuclein
0.159
ATP
pH 7.8, 22°C, recombinant mutant F255Y
0.16
ATP
recombinant mutant enzyme V241I/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.16
ATP
recombinant wild type enzyme, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.16
ATP
wild type enzyme, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.16
ATP
wild-type, in the presence of 0.001 mM D-luciferin
0.1602
ATP
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.166
ATP
recombinant mutant enzyme F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.182
ATP
recombinant mutant enzyme V241I/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.2
ATP
-
phosphate buffer
0.2
ATP
-
25°C, pH 8.5, mutant I232R
0.2
ATP
-
35°C, pH 8, mutant A296C/A326C/I232R
0.215
ATP
recombinant mutant enzyme F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.23
ATP
-
wild-type enzyme
0.283
ATP
recombinant mutant enzyme V241I, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.285
ATP
-
glycylglycine buffer
0.7
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][propionate]
1.666
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
2.25
ATP
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
6.9
ATP
-
N-terminal domain
83
ATP
pH and temperature not specified in the publication, wild-type enzyme
88
ATP
pH and temperature not specified in the publication, mutant enzyme L300K
100
ATP
pH and temperature not specified in the publication, mutant enzyme L300R
140
ATP
pH and temperature not specified in the publication, mutant enzyme L300E
0.00076
D-firefly luciferin
25°C, pH 7.8, I423L/D436G/L530R
0.00121
D-firefly luciferin
25°C, pH 7.8, wild-type enzyme
0.002
D-firefly luciferin
pH 7.8, temperature not specified in the publication, mutant enzyme H489K
0.0023
D-firefly luciferin
pH 7.8, temperature not specified in the publication, mutant enzyme H489M
0.00244
D-firefly luciferin
pH 8.0, 25°C
0.0025
D-firefly luciferin
pH 7.8, temperature not specified in the publication, mutant enzyme H489D
0.0025
D-firefly luciferin
Amydetes vivianii
pH 8.0, 22°C, mutant enzyme E270A
0.003
D-firefly luciferin
-
pH 8.0, temperature not specified in the publication, isoenzyme AL2
0.004
D-firefly luciferin
Amydetes vivianii
pH 8.0, 22°C, mutant enzyme E270G
0.0042
D-firefly luciferin
25°C, pH 7.8, mutant enzyme T214A/A215L/I232A/F295L/E345K/I423L/D436G/L530R
0.005
D-firefly luciferin
pH 7.8, temperature not specified in the publication, mutant enzyme H461D
0.005
D-firefly luciferin
pH 7.8, temperature not specified in the publication, wild-type enzyme
0.006
D-firefly luciferin
pH 7.8, 25°C, wild-type enzyme
0.007
D-firefly luciferin
-
pH 8.0, temperature not specified in the publication, isoenzyme AL1
0.00881
D-firefly luciferin
25°C, pH 7.8, mutant enzyme T214A/A215L/I232A/F295L/E345K
0.009
D-firefly luciferin
Amydetes vivianii
pH 8.0, 22°C, wild-type enzyme
0.014
D-firefly luciferin
pH 7.8, 22°C, recombinant mutant Y255F
0.015
D-firefly luciferin
pH 7.8, 22°C, recombinant mutant F255Y
0.015
D-firefly luciferin
pH 7.8, 22°C, recombinant wild-type enzyme
0.018
D-firefly luciferin
pH 8.0, 25°C
0.019
D-firefly luciferin
pH 7.8, 22°C, recombinant wild-type enzyme
0.0225
D-firefly luciferin
pH 7.8, 25°C, mutant enzyme K329I
0.023
D-firefly luciferin
pH 7.5, temperature not specified in the publication
0.024
D-firefly luciferin
pH 7.8, 22°C, recombinant mutant R213K/T214N
0.04639
D-firefly luciferin
pH 7.5, 25°C
0.061
D-firefly luciferin
pH 7.5, 25°C
0.1421
D-firefly luciferin
pH 7.8, 25°C, mutant enzyme R330Q
10
D-firefly luciferin
pH and temperature not specified in the publication, mutant enzyme L300K
12.5
D-firefly luciferin
pH and temperature not specified in the publication, wild-type enzyme
14
D-firefly luciferin
pH and temperature not specified in the publication, mutant enzyme L300R
25
D-firefly luciferin
pH and temperature not specified in the publication, mutant enzyme L300E
0.001
D-luciferin
wild type enzyme, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.001
D-luciferin
mutant I423L/D436G/L530R, in the presence of 0.01 mM ATP
0.0018
D-luciferin
mutant enzyme D436G, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.002
D-luciferin
mutant enzyme D436G, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.002
D-luciferin
mutant D436G, in the presence of 0.01 mM ATP
0.0023
D-luciferin
mutant enzyme K443A
0.0024
D-luciferin
native luciferase
0.0024
D-luciferin
native luciferase
0.0037
D-luciferin
mutant enzyme L530R, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.004
D-luciferin
mutant enzyme I423L, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.004
D-luciferin
mutant enzyme L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.004
D-luciferin
recombinant mutant enzyme G246A, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.004
D-luciferin
mutant I423L, in the presence of 0.01 mM ATP
0.004
D-luciferin
mutant L530R, in the presence of 0.01 mM ATP
0.0042
D-luciferin
-
mutant enzyme G246A
0.0043
D-luciferin
mutant enzyme I432L, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.0047
D-luciferin
recombinant luciferase
0.0047
D-luciferin
recombinant luciferase
0.006
D-luciferin
mutant enzyme G446I
0.006
D-luciferin
mutant enzyme Q448A
0.006
D-luciferin
recombinant mutant enzyme V241I/G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.006
D-luciferin
mutant ins356E
0.008
D-luciferin
recombinant mutant enzyme V241I, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.008
D-luciferin
-
mutant D476N, pH 7, 25°C
0.0089
D-luciferin
mutant enzyme K445Q
0.009
D-luciferin
recombinant mutant enzyme V241I/G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.009
D-luciferin
mutant ins356K
0.01
D-luciferin
recombinant mutant enzyme G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.01
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][acetate]
0.01
D-luciferin
-
pH 7.8, temperature not specified in the publication, native enzyme
0.011
D-luciferin
recombinant mutant enzyme G246A/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.011
D-luciferin
recombinant mutant enzyme G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.011
D-luciferin
mutant E354K/ins356K
0.011
D-luciferin
wild-type luciferase
0.012
D-luciferin
recombinant mutant enzyme V241I/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.012
D-luciferin
mutant E354Q/ins356K
0.0125
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][lactate]
0.013
D-luciferin
mutant E354K
0.014
D-luciferin
recombinant mutant enzyme F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.014
D-luciferin
mutant E354R/ins356K
0.015
D-luciferin
-
wild-type enzyme
0.015
D-luciferin
wild-type enzyme
0.015
D-luciferin
-
mutant enzyme H245A
0.015
D-luciferin
recombinant wild type enzyme, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.015
D-luciferin
mutant ins356R
0.015
D-luciferin
-
wild-type, pH 8, 25°C
0.0157
D-luciferin
-
mutant enzyme F250G
0.016
D-luciferin
recombinant mutant enzyme F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.016
D-luciferin
mutant E354R
0.016
D-luciferin
-
mutant D474K, pH 8.5, 25°C
0.01612
D-luciferin
wild-type luciferase
0.018
D-luciferin
-
mutant enzyme F247Y
0.018
D-luciferin
-
mutant enzyme G316A
0.018
D-luciferin
mutant ins356Q
0.02
D-luciferin
at pH 7.8, in 50 mM Tricine-NaOH buffer with 10 mM MgSO4
0.02
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
0.021
D-luciferin
mutant enzyme I423L/D436G/L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2
0.021
D-luciferin
wild-type, in the presence of 0.001 mM D-luciferin
0.0211
D-luciferin
wild type enzyme, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2
0.022
D-luciferin
-
mutant enzyme F250S
0.022
D-luciferin
recombinant mutant enzyme F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.023
D-luciferin
mutant H245N
0.023
D-luciferin
wild-type luciferase
0.024
D-luciferin
recombinant mutant enzyme V241I/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.024
D-luciferin
recombinant mutant enzyme V241I/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C
0.026
D-luciferin
mutant H431Y
0.028
D-luciferin
-
pH 8.2, temperature not specified in the publication
0.03
D-luciferin
at pH 7.8, in 50 mM Tricine-NaOH buffer with 10 mM MgSO4
0.03
D-luciferin
mutant S284T
0.06
D-luciferin
-
mutant enzyme G341A
0.0625
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][lactate]
0.067
D-luciferin
mutant enzyme K443A/K529A
0.07
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
0.085
D-luciferin
-
mutant enzyme I351A
0.099
D-luciferin
-
mutant enzyme T343A
0.1
D-luciferin
-
35°C, pH 8.5, mutant A296C/A326C
0.124
D-luciferin
-
mutant enzyme F247L
0.125
D-luciferin
-
25°C, pH 8, wild-type
0.13
D-luciferin
-
mutant enzyme L342A
0.133
D-luciferin
-
mutant enzyme A348V
0.17
D-luciferin
-
mutant enzyme S347A
0.2
D-luciferin
-
mutant enzyme G315A
0.2
D-luciferin
-
25°C, pH 8.5, mutant I232R
0.2
D-luciferin
-
35°C, pH 8, mutant A296C/A326C/I232R
0.2
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.125 M [1,1,3,3-tetramethylguanidine][propionate]
0.23
D-luciferin
-
mutant enzyme F247A
0.23
D-luciferin
-
mutant enzyme K529A
0.23
D-luciferin
mutant enzyme K529A
0.301
D-luciferin
-
mutant enzyme R218A
0.311
D-luciferin
-
mutant enzyme T251A
0.5
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][triflouroacetate]
1
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][acetate]
1
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][propionate]
2.5
D-luciferin
-
pH 7.8, temperature not specified in the publication, 0.5 M [1,1,3,3-tetramethylguanidine][trichloroacetate]
0.00038
D-luciferyl-O-adenosine monophosphate
mutant enzyme K443A
0.00055
D-luciferyl-O-adenosine monophosphate
mutant enzyme K443A/K529A
0.0015
D-luciferyl-O-adenosine monophosphate
mutant enzyme G446I
0.0022
D-luciferyl-O-adenosine monophosphate
mutant enzyme Q448A
0.0039
D-luciferyl-O-adenosine monophosphate
mutant enzyme K445Q
0.0047
D-luciferyl-O-adenosine monophosphate
wild-type enzyme
0.0126
D-luciferyl-O-adenosine monophosphate
mutant enzyme K529A
0.00741
lauric acid
-
0.0072
Luciferin
-
wild-type enzyme
0.0079
Luciferin
-
addition of luciferin 30 min before ATP
0.008
Luciferin
free enzyme, in 0.02 M Tris-acetate buffer, pH 7.8, containing 12 mM magnesium acetate, 0.2 mM EDTA, and 0.3 mM dithiothreitol
0.0083
Luciferin
-
addition of luciferin 30 min after ATP
0.01
Luciferin
-
mutant R213M
0.012
Luciferin
-
immobilized on activated Sepharose
0.012
Luciferin
-
90 microM ATP
0.012
Luciferin
-
wild-type luciferase
0.013
Luciferin
-
mutant Q338P
0.014
Luciferin
-
mutant R213E
0.016
Luciferin
-
90 microM ATP, presence of 0.1 microM of N-quinolin-2-ylbenzamide
0.018
Luciferin
-
mutant R337Q
0.026
Luciferin
-
N-terminal domain
0.042
Luciferin
-
phosphate buffer
0.053
Luciferin
-
90 microM ATP, presence of 1 microM of N-quinolin-2-ylbenzamide
0.055
Luciferin
-
glycylglycine buffer
0.074
Luciferin
-
0.5 mM ATP, in presence of alpha-synuclein
0.088
Luciferin
-
0.2 mM ATP, in presence of alpha-synuclein
0.134
Luciferin
-
0.15 mM ATP, in presence of alpha-synuclein
0.188
Luciferin
-
0.15 mM ATP, without alpha-synuclein
0.189
Luciferin
-
0.5 mM ATP, without alpha-synuclein
0.192
Luciferin
-
0.2 mM ATP, without alpha-synuclein
0.197
Luciferin
-
0.1 mM ATP, without alpha-synuclein
0.218
Luciferin
-
0.1 mM ATP, in presence of alpha-synuclein
0.0006
luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme A243G
0.0008
luciferyl-O-adenosine monophosphate
-
pH 8.6, wild-type enzyme
0.0046
luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme S247F
0.0077
luciferyl-O-adenosine monophosphate
-
pH 8.6, wild-type enzyme
0.0114
luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme F250S
0.0127
luciferyl-O-adenosine monophosphate
-
pH 8.6, mutant enzyme G246A
0.025
MgATP2-
-
-
0.029
MgATP2-
-
mutant enzyme G246A
0.0486
MgATP2-
mutant enzyme K443A
0.069
MgATP2-
mutant enzyme K445Q
0.073
MgATP2-
mutant enzyme G446I
0.08
MgATP2-
-
mutant enzyme F247Y
0.107
MgATP2-
-
mutant enzyme G316A
0.133
MgATP2-
-
mutant enzyme F250S
0.16
MgATP2-
-
wild-type enzyme
0.16
MgATP2-
wild-type enzyme
0.166
MgATP2-
-
mutant enzyme F250G
0.2
MgATP2-
-
mutant enzyme G341A
0.226
MgATP2-
-
mutant enzyme F247L
0.24
MgATP2-
-
mutant enzyme H245A
0.285
MgATP2-
-
mutant enzyme I351A
0.341
MgATP2-
mutant enzyme Q448A
0.344
MgATP2-
-
mutant enzyme S347A
0.56
MgATP2-
mutant enzyme K443A/K529A
0.857
MgATP2-
-
mutant enzyme T343A
1.038
MgATP2-
-
mutant enzyme A348V
1.2
MgATP2-
-
mutant enzyme G315A
1.2
MgATP2-
-
mutant enzyme K529A
1.2
MgATP2-
mutant enzyme K529A
1.2
MgATP2-
-
mutant enzyme L342A
2
MgATP2-
-
mutant enzyme T251A
3.5
MgATP2-
-
mutant enzyme F247A
6.2
MgATP2-
-
mutant enzyme R218A
additional information
additional information
-
increase of the Km with increasing ionic strength
-
additional information
additional information
the Km value for the reaction intermediate D-firefly luciferin-AMP is 0.14 mM
-
additional information
additional information
-
the Km value for the reaction intermediate D-firefly luciferin-AMP is 0.14 mM
-
additional information
additional information
the Km value for the reaction intermediate D-firefly luciferin-AMP is 0.24 mM
-
additional information
additional information
-
the Km value for the reaction intermediate D-firefly luciferin-AMP is 0.24 mM
-
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0.0004
(2E)-1-(1-benzofuran-2-yl)-3-(4-methylphenyl)prop-2-en-1-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0018
(2E)-1-(1-benzofuran-2-yl)-3-phenylprop-2-en-1-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.00007
(2E)-1-(2-hydroxyphenyl)-3-(4-methylphenyl)prop-2-en-1-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0011
(2E)-1-(5-chlorothiophen-2-yl)-3-(4-methylphenyl)prop-2-en-1-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.00041
(2E)-1-(5-chlorothiophen-2-yl)-3-phenylprop-2-en-1-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.000088
(2E)-2-benzylidene-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
0.0002
(2E)-2-[(2-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.00009
(2E)-2-[(2-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0005
(2E)-2-[(2-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.00044
(2E)-2-[(2-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0013
(2E)-2-[(2-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0006
(2E)-2-[(3-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0014
(2E)-2-[(3-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.000034
(2E)-2-[(3-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0015
(2E)-2-[(3-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0011
(2E)-2-[(3-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.000007
(2E)-2-[(4-bromophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.00006
(2E)-2-[(4-chlorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.000007
(2E)-2-[(4-ethoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0000012
(2E)-2-[(4-ethylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.000031
(2E)-2-[(4-fluorophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one, (2E)-2-[(4-hydroxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0000012
(2E)-2-[(4-methoxyphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0000005
(2E)-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.000056
(2E)-2-[(4-nitrophenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0109
(2E)-2-[(pyridin-3-yl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.00013
(2E)-2-[[4-(benzyloxy)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.000049
(2E)-2-[[4-(diethylamino)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0000005
(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0002
(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-6-methoxy-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0012
(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-7-methoxy-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.007
(2E)-2-[[4-(dimethylamino)phenyl]methylidene]-8-methoxy-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.000012
(2E)-2-[[4-(methylsulfanyl)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.00026
(2E)-2-[[4-(trifluoromethyl)phenyl]methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.00014
(2E)-5-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.000159
(2E)-6-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.00286 - 122
(2E)-7-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
-
0.000106
(2E)-8-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0002
(2R)-2-[4-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)phenyl]propanoic acid
Photinus pyralis
-
0.002
(2Z)-1-(4-chlorophenyl)-3-(pyridin-2-ylamino)prop-2-en-1-one
Photinus pyralis
-
0.00008
(2Z)-3-[(2-bromophenyl)amino]-1-pyridin-2-ylprop-2-en-1-one
Photinus pyralis
-
0.001
(2Z)-3-[(4-fluorophenyl)amino]-1-furan-2-ylprop-2-en-1-one
Photinus pyralis
-
0.00021
(2Z)-3-[[4-(dimethylamino)cyclohexa-1,5-dien-1-yl]amino]-1-phenylprop-2-en-1-one
Photinus pyralis
-
0.0008
(3Z)-3-[[4-(dimethylamino)phenyl]methylidene]-1,3-dihydro-2H-indol-2-one
Photinus pyralis
-
0.00000025
(6E)-6-[(3-carboxy-4-hydroxyphenyl)methylidene]-5-oxo-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
Photinus pyralis
pH and temperature not specified in the publication
-
0.002
(7E)-7-[(4-methylphenyl)methylidene]-8-oxo-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
Photinus pyralis
pH and temperature not specified in the publication
-
0.0006
1-[3-(6-ethoxy-1,3-benzothiazol-2-yl)thiophen-2-yl]urea
Photinus pyralis
-
0.00008
2,4-dimethoxy-N-(5-methylpyridin-2-yl)benzamide
Photinus pyralis
-
0.0062
2-(2-amino-3-methoxyphenyl)-4H-chromen-4-one
Photinus pyralis
-
0.0049 - 0.0054
2-(2-chlorophenyl)-6-methoxy-1,3-benzothiazole
-
0.0005 - 0.0006
2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole
0.00032
2-(2-imino-4,5,6,7-tetrahydro-1,3-benzothiazol-3(2H)-yl)-1-(4-methylphenyl)ethanone
Photinus pyralis
-
0.0077 - 0.0113
2-(2-methoxyphenyl)-1,3-benzothiazole
0.0019 - 0.0032
2-(3,4-dimethoxyphenyl)-1,3-benzothiazole
0.0028 - 0.0038
2-(3,4-dimethoxyphenyl)-6-methoxy-1,3-benzothiazole
0.0078 - 0.0242
2-(3-fluorophenyl)-1,3-benzothiazole
0.0011 - 0.0015
2-(3-fluorophenyl)-6-methoxy-1,3-benzothiazole
0.0014 - 0.0045
2-(4-chlorophenyl)-1,3-benzothiazole
0.0035 - 0.0038
2-(4-chlorophenyl)-6-methoxy-1,3-benzothiazole
0.0013
2-(4-ethoxyphenyl)-4-[(4-methylpiperazin-1-yl)carbonyl]quinoline
Photinus pyralis
-
0.00041
2-(4-ethoxyphenyl)-4-[(4-pyridin-2-ylpiperazin-1-yl)carbonyl]quinoline
Photinus pyralis
-
0.00086 - 0.0013
2-(4-fluorophenyl)-6-methoxy-1,3-benzothiazole
0.00036 - 0.001
2-(4-methoxyphenyl)-1,3-benzothiazole
0.004
2-(4-methylphenyl)-4-[(4-pyrimidin-2-ylpiperazin-1-yl)carbonyl]quinoline
Photinus pyralis
-
0.000038 - 0.0001
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
0.0013 - 0.0171
2-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
0.0001
2-(5-naphthalen-2-yl-1,2,4-oxadiazol-3-yl)pyridine
Photinus pyralis
-
0.0019 - 0.0144
2-(5-pyridin-4-yl-1,2,4-oxadiazol-3-yl)pyridine
0.0073
2-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00016
2-benzylidene-1H-indene-1,3(2H)-dione
Photinus pyralis
pH and temperature not specified in the publication
-
0.00056
2-hydroxy-5-[(E)-(1-oxo-3,4-dihydronaphthalen-2(1H)-ylidene)methyl]benzoic acid
Photinus pyralis
pH and temperature not specified in the publication
-
0.0008
2-hydroxy-N'-[(1E)-(2-hydroxyphenyl)methylidene]benzohydrazide
Photinus pyralis
-
0.0047
2-methyl-6-(phenylethynyl)pyridine
Photinus pyralis
-
0.0043
2-methyl-6-[(Z)-2-phenylethenyl]pyridine
Photinus pyralis
-
0.000063
2-[(4-methylphenyl)methylidene]-1H-indene-1,3(2H)-dione
Photinus pyralis
pH and temperature not specified in the publication
-
0.0024
2-[(4-methylphenyl)methyl]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.00008 - 0.0028
2-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]pyridine
0.00084
2-[5-(3,4-dichlorophenyl)-1,2,4-oxadiazol-3-yl]pyridine
Photinus pyralis
-
0.00022
2-[5-(3-chloro-4-methylphenyl)-1,2,4-oxadiazol-3-yl]pyridine
Photinus pyralis
-
0.0005
2-[5-(3-chlorophenyl)-1,2,4-oxadiazol-3-yl]pyridine
Photinus pyralis
-
0.0032
2-[5-(5-bromofuran-2-yl)-1,2,4-oxadiazol-3-yl]pyridine
Photinus pyralis
-
0.0018
2-[[4-(dimethylamino)phenyl]methyl]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.00005
3-(2-hydroxyphenyl)-1H-benzo[f]chromen-1-one
Photinus pyralis
-
0.0006 - 0.0083
3-(2-methoxyphenyl)-5-phenyl-1,2,4-oxadiazole
0.00058
3-(4-methylphenyl)-4,5-dihydro-2H-benzo[g]indazole
Photinus pyralis
pH and temperature not specified in the publication
-
0.01471
3-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00016
3-chloro-N-(5-phenylpyridin-2-yl)benzamide
Luciola mingrelica
-
-
0.00004 - 0.0014
3-pyridin-2-yl-1,2,4-oxadiazol-5-yl biphenyl-4-carboxylate
0.0002 - 0.00032
4-(1,3-benzothiazol-2-yl)-N,N-dimethylaniline
0.0021 - 0.0063
4-(1,3-benzothiazol-2-yl)benzonitrile
0.0007
4-(1,4-dioxa-8-azaspiro[4.5]dec-8-ylcarbonyl)-2-(4-ethoxyphenyl)quinoline
Photinus pyralis
-
0.01076
4-(4-aminophenoxy)-7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-2-amine
Photinus pyralis
-
pH 7.8, 20°C
0.0059
4-(4-methylphenyl)-5,6-dihydrobenzo[h]quinazolin-2-amine
Photinus pyralis
pH and temperature not specified in the publication
-
0.0024 - 0.024
4-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
0.0007 - 0.0027
4-(6-methoxy-1,3-benzothiazol-2-yl)-N,N-dimethylaniline
0.0057 - 0.0061
4-(6-methoxy-1,3-benzothiazol-2-yl)benzonitrile
0.00012
4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)-N,N-dimethylaniline
Photinus pyralis
-
pH 7.8, 20°C
0.00007
4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)-N-methylaniline
Photinus pyralis
-
pH 7.8, 20°C
0.00008
4-([7-(2,2-dimethylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00012
4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00031
4-([7-(2-methylpropyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00753
4-([7-(3-methylbut-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00646
4-([7-(3-methylbutyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00224
4-([7-(prop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00036
4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.0017
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
Photinus pyralis
-
0.0012
4-amino-N-(5-phenylpyridin-2-yl)benzamide
Luciola mingrelica
-
-
0.00041
4-methoxy-N-[(4-methylpyridin-2-yl)carbamoyl]benzamide
Photinus pyralis
-
0.00029
4-[(7-cyclopentyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00943
4-[(7-ethenyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00351
4-[(7-ethyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)oxy]aniline
Photinus pyralis
-
pH 7.8, 20°C
0.0003
4-[1-(1,3-benzothiazol-2-yl)-2-(4-methylpiperazin-1-yl)-2-oxoethyl]phenol
Photinus pyralis
-
0.0048 - 0.024
4-[3-(2-methoxyphenyl)-1,2,4-oxadiazol-5-yl]pyridine
0.00032 - 0.0005
4-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]-N,N-dimethylaniline
0.000033
5'-O-[[2-(6-hydroxy-1,3-benzothiazol-2-yl)-1,3-thiazole-4-carbonyl]sulfamoyl]adenosine
Photinus pyralis
pH and temperature not specified in the publication
-
0.000054 - 0.0002
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
0.001
5-(2-bromophenyl)-3-(4-methylphenyl)-1,2,4-oxadiazole
Photinus pyralis
-
0.00015
5-(2-chloro-4-methylphenyl)-3-phenyl-1,2,4-oxadiazole
Photinus pyralis
-
0.0003 - 0.0028
5-(2-fluorophenyl)-3-(4-methoxyphenyl)-1,2,4-oxadiazole
0.00058 - 0.0017
5-(4-fluorophenyl)-3-(3-methylphenyl)-1,2,4-oxadiazole
0.0003
5-(ethanesulfonyl)-2-(naphthalen-2-yl)-1,3-benzoxazole
Photinus pyralis
pH and temperature not specified in the publication
-
0.0011
5-methyl-N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide
Photinus pyralis
-
0.00041
5-naphthalen-2-yl-3-phenyl-1,2,4-oxadiazole
Photinus pyralis
-
0.0002
5-[(2E)-4-(4-bromophenyl)-4-oxobut-2-en-1-yl]-2-hydroxybenzoic acid
Photinus pyralis
pH and temperature not specified in the publication
-
0.00044
5-[(E)-(6-bromo-1-oxo-3,4-dihydronaphthalen-2(1H)-ylidene)methyl]-2-hydroxybenzoic acid
Photinus pyralis
pH and temperature not specified in the publication
-
0.0032 - 0.0056
6-methoxy-2-(2-methoxyphenyl)-1,3-benzothiazole
0.00067 - 0.0015
6-methoxy-2-(3-methylphenyl)-1,3-benzothiazole
0.0022 - 0.0041
6-methoxy-2-(4-methoxyphenyl)-1,3-benzothiazole
0.0043 - 0.0089
6-methoxy-2-[2-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
0.0134 - 0.03
6-methoxy-2-[3-(2-methylbenzyl)phenyl]-1,3-benzothiazole
-
0.0045
6-methyl-2-[(Z)-phenyldiazenyl]pyridin-3-ol
Photinus pyralis
-
13.6
butanoic acid
Photinus pyralis
-
IC50: 13.6 mM
0.135
D-luciferin
Photinus pyralis
-
inhibits CoA-ligase activity with L-luciferin, IC50: 0.135 mM against 0.1 mM L-luciferin
0.0132
Decanoic acid
Photinus pyralis
-
IC50: 0.0132 mM
0.000006
dehydroluciferyl adenylate
Photinus pyralis
-
IC50: 6 nM
0.0000074 - 0.000022
dehydroluciferyl-adenylate
0.005
dehydroluciferyl-CoA
Photinus pyralis
-
IC50: 0.005 mM
0.0012
dodecanoic acid
Photinus pyralis
-
IC50: 0.0012 mM
0.0009
ethyl 4-[[2-(4-ethoxyphenyl)quinolin-4-yl]carbonyl]piperazine-1-carboxylate
Photinus pyralis
-
0.00067
hexadecanoic acid
Photinus pyralis
-
IC50: 0.00067 mM
3.4
hexanoic acid
Photinus pyralis
-
IC50: 3.4 mM
0.00005
lipoic acid
Photinus pyralis
-
0.00068
myristic acid
Photinus pyralis
-
0.0045
N'-(3-chlorophenyl)-N-[(1Z)-(3-chlorophenyl)methylidene]imidoformamide
Photinus pyralis
-
0.00009
N,N-dimethyl-4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00018
N,N-dimethyl-4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.0006
N-(4-ethoxyphenyl)-2-methoxybenzamide
Photinus pyralis
-
0.0064
N-(5-methylpyridin-2-yl)benzamide
Luciola mingrelica
-
-
0.000069
N-(5-phenylpyridin-2-yl)benzamide
Luciola mingrelica
-
-
0.0024
N-(5-phenylpyridin-2-yl)cyclohexanecarboxamide
Luciola mingrelica
-
-
0.00065
N-(6-ethoxy-1,3-benzothiazol-2-yl)-2-methylfuran-3-carboxamide
Photinus pyralis
-
0.0012
N-(6-methoxy-1,3-benzothiazol-2-yl)-2-methylfuran-3-carboxamide
Photinus pyralis
-
0.0005
N-(6-methyl-1,3-benzothiazol-2-yl)thiophene-2-carboxamide
Photinus pyralis
-
0.00006
N-methyl-4-([7-(2-methylprop-2-en-1-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.00013
N-methyl-4-([7-(propan-2-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]oxy)aniline
Photinus pyralis
-
pH 7.8, 20°C
0.000069
N-pyridin-2-ylbenzamide
Photinus pyralis
-
0.007
N-quinolin-2-ylbenzamide
Luciola mingrelica
-
-
0.0019 - 0.0029
N-[3-(6-methoxy-1,3-benzothiazol-2-yl)phenyl]acetamide
0.003 - 0.0031
N-[4-(1,3-benzothiazol-2-yl)phenyl]acetamide
0.00056
N-[5-(4-chlorophenyl)pyridin-2-yl]benzamide
Luciola mingrelica
-
-
0.00031
N-[5-(4-methoxyphenyl)pyridin-2-yl]benzamide
Luciola mingrelica
-
-
0.0007
N-[5-[(2,2-dimethylpropanoyl)amino]pyridin-2-yl]-3-hydroxybenzamide
Photinus pyralis
-
0.0011
N-[6-(methylsulfonyl)-1,3-benzothiazol-2-yl]thiophene-2-carboxamide
Photinus pyralis
-
0.001
NFkappaBAI4
Photinus pyralis
pH and temperature not specified in the publication
-
0.00063
octadecanoic acid
Photinus pyralis
-
IC50: 0.00063 mM
2.9
octanoic acid
Photinus pyralis
-
IC50: 2.9 mM
0.0019 - 0.002
resveratrol
0.00068
tetradecanoic acid
Photinus pyralis
-
IC50: 0.00068 mM
0.0005
[2-(4-ethoxyphenyl)quinolin-4-yl][4-(pyridin-2-yl)piperazin-1-yl]methanone
Photinus pyralis
pH and temperature not specified in the publication
-
0.00286
(2E)-7-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
122
(2E)-7-methoxy-2-[(4-methylphenyl)methylidene]-3,4-dihydronaphthalen-1(2H)-one
Photinus pyralis
pH and temperature not specified in the publication
-
0.0049
2-(2-chlorophenyl)-6-methoxy-1,3-benzothiazole
Photuris pensylvanica
-
-
-
0.0054
2-(2-chlorophenyl)-6-methoxy-1,3-benzothiazole
Photinus pyralis
-
-
-
0.0005
2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole
Photuris pensylvanica
-
-
0.0005
2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole
Photinus pyralis
pH and temperature not specified in the publication
0.0006
2-(2-fluorophenyl)-6-methoxy-1,3-benzothiazole
Photinus pyralis
-
-
0.0077
2-(2-methoxyphenyl)-1,3-benzothiazole
Photuris pensylvanica
-
-
0.0113
2-(2-methoxyphenyl)-1,3-benzothiazole
Photinus pyralis
-
-
0.0019
2-(3,4-dimethoxyphenyl)-1,3-benzothiazole
Photuris pensylvanica
-
-
0.0032
2-(3,4-dimethoxyphenyl)-1,3-benzothiazole
Photinus pyralis
-
-
0.0028
2-(3,4-dimethoxyphenyl)-6-methoxy-1,3-benzothiazole
Photinus pyralis
-
-
0.0038
2-(3,4-dimethoxyphenyl)-6-methoxy-1,3-benzothiazole
Photuris pensylvanica
-
-
0.0078
2-(3-fluorophenyl)-1,3-benzothiazole
Photuris pensylvanica
-
-
0.0242
2-(3-fluorophenyl)-1,3-benzothiazole
Photinus pyralis
-
-
0.0011
2-(3-fluorophenyl)-6-methoxy-1,3-benzothiazole
Photuris pensylvanica
-
-
0.0015
2-(3-fluorophenyl)-6-methoxy-1,3-benzothiazole
Photinus pyralis
-
-
0.0014
2-(4-chlorophenyl)-1,3-benzothiazole
Photuris pensylvanica
-
-
0.0045
2-(4-chlorophenyl)-1,3-benzothiazole
Photinus pyralis
-
-
0.0035
2-(4-chlorophenyl)-6-methoxy-1,3-benzothiazole
Photinus pyralis
-
-
0.0038
2-(4-chlorophenyl)-6-methoxy-1,3-benzothiazole
Photuris pensylvanica
-
-
0.00086
2-(4-fluorophenyl)-6-methoxy-1,3-benzothiazole
Photuris pensylvanica
-
-
0.0013
2-(4-fluorophenyl)-6-methoxy-1,3-benzothiazole
Photinus pyralis
-
-
0.00036
2-(4-methoxyphenyl)-1,3-benzothiazole
Photuris pensylvanica
-
-
0.001
2-(4-methoxyphenyl)-1,3-benzothiazole
Photinus pyralis
-
-
0.000038
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
Photuris pensylvanica
-
-
0.00008
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
Photinus pyralis
-
-
0.0001
2-(5-biphenyl-4-yl-1,2,4-oxadiazol-3-yl)pyridine
Photinus pyralis
-
0.0013
2-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
Photuris pensylvanica
-
-
0.0171
2-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
Photinus pyralis
-
-
0.0019
2-(5-pyridin-4-yl-1,2,4-oxadiazol-3-yl)pyridine
Photuris pensylvanica
-
-
0.0144
2-(5-pyridin-4-yl-1,2,4-oxadiazol-3-yl)pyridine
Photinus pyralis
-
-
0.00008
2-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]pyridine
Photuris pensylvanica
-
-
0.0028
2-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]pyridine
Photinus pyralis
-
-
0.0006
3-(2-methoxyphenyl)-5-phenyl-1,2,4-oxadiazole
Photuris pensylvanica
-
-
0.0083
3-(2-methoxyphenyl)-5-phenyl-1,2,4-oxadiazole
Photinus pyralis
-
-
0.00004
3-pyridin-2-yl-1,2,4-oxadiazol-5-yl biphenyl-4-carboxylate
Photuris pensylvanica
-
-
0.0014
3-pyridin-2-yl-1,2,4-oxadiazol-5-yl biphenyl-4-carboxylate
Photinus pyralis
-
-
0.0002
4-(1,3-benzothiazol-2-yl)-N,N-dimethylaniline
Photinus pyralis
-
-
0.00032
4-(1,3-benzothiazol-2-yl)-N,N-dimethylaniline
Photuris pensylvanica
-
-
0.0021
4-(1,3-benzothiazol-2-yl)benzonitrile
Photuris pensylvanica
-
-
0.0063
4-(1,3-benzothiazol-2-yl)benzonitrile
Photinus pyralis
-
-
0.0024
4-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
Photuris pensylvanica
-
-
0.024
4-(5-furan-2-yl-1,2,4-oxadiazol-3-yl)pyridine
Photinus pyralis
-
-
0.0007
4-(6-methoxy-1,3-benzothiazol-2-yl)-N,N-dimethylaniline
Photinus pyralis
-
-
0.0027
4-(6-methoxy-1,3-benzothiazol-2-yl)-N,N-dimethylaniline
Photuris pensylvanica
-
-
0.0057
4-(6-methoxy-1,3-benzothiazol-2-yl)benzonitrile
Photinus pyralis
-
-
0.0061
4-(6-methoxy-1,3-benzothiazol-2-yl)benzonitrile
Photuris pensylvanica
-
-
0.0048
4-[3-(2-methoxyphenyl)-1,2,4-oxadiazol-5-yl]pyridine
Photuris pensylvanica
-
-
0.024
4-[3-(2-methoxyphenyl)-1,2,4-oxadiazol-5-yl]pyridine
Photinus pyralis
-
-
0.00032
4-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]-N,N-dimethylaniline
Photuris pensylvanica
-
-
0.0005
4-[5-(2-methoxyphenyl)-1,2,4-oxadiazol-3-yl]-N,N-dimethylaniline
Photinus pyralis
-
-
0.000054
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
Photuris pensylvanica
-
-
0.00015
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
Photinus pyralis
-
0.0002
5-(2,4-dimethoxyphenyl)-3-phenyl-1,2,4-oxadiazole
Photinus pyralis
-
-
0.0003
5-(2-fluorophenyl)-3-(4-methoxyphenyl)-1,2,4-oxadiazole
Photuris pensylvanica
-
-
0.0028
5-(2-fluorophenyl)-3-(4-methoxyphenyl)-1,2,4-oxadiazole
Photinus pyralis
-
-
0.00058
5-(4-fluorophenyl)-3-(3-methylphenyl)-1,2,4-oxadiazole
Photuris pensylvanica
-
-
0.0017
5-(4-fluorophenyl)-3-(3-methylphenyl)-1,2,4-oxadiazole
Photinus pyralis
-
-
0.0032
6-methoxy-2-(2-methoxyphenyl)-1,3-benzothiazole
Photinus pyralis
-
-
0.0056
6-methoxy-2-(2-methoxyphenyl)-1,3-benzothiazole
Photuris pensylvanica
-
-
0.00067
6-methoxy-2-(3-methylphenyl)-1,3-benzothiazole
Photuris pensylvanica
-
-
0.0015
6-methoxy-2-(3-methylphenyl)-1,3-benzothiazole
Photinus pyralis
-
-
0.0022
6-methoxy-2-(4-methoxyphenyl)-1,3-benzothiazole
Photinus pyralis
-
-
0.0041
6-methoxy-2-(4-methoxyphenyl)-1,3-benzothiazole
Photuris pensylvanica
-
-
0.0043
6-methoxy-2-[2-(2-methylbenzyl)phenyl]-1,3-benzothiazole
Photuris pensylvanica
-
-
-
0.0089
6-methoxy-2-[2-(2-methylbenzyl)phenyl]-1,3-benzothiazole
Photinus pyralis
-
-
-
0.0134
6-methoxy-2-[3-(2-methylbenzyl)phenyl]-1,3-benzothiazole
Photinus pyralis
-
-
-
0.03
6-methoxy-2-[3-(2-methylbenzyl)phenyl]-1,3-benzothiazole
Photuris pensylvanica
-
-
-
0.0000074
dehydroluciferyl-adenylate
Photinus pyralis
-
2.5 nM D-luciferin
0.0000085
dehydroluciferyl-adenylate
Photinus pyralis
-
5 nM D-luciferin
0.0000103
dehydroluciferyl-adenylate
Photinus pyralis
-
10 nM D-luciferin
0.0000132
dehydroluciferyl-adenylate
Photinus pyralis
-
20 nM D-luciferin
0.000022
dehydroluciferyl-adenylate
Photinus pyralis
-
40 nM D-luciferin
0.0019
N-[3-(6-methoxy-1,3-benzothiazol-2-yl)phenyl]acetamide
Photuris pensylvanica
-
-
0.0029
N-[3-(6-methoxy-1,3-benzothiazol-2-yl)phenyl]acetamide
Photinus pyralis
-
-
0.003
N-[4-(1,3-benzothiazol-2-yl)phenyl]acetamide
Photinus pyralis
-
-
0.0031
N-[4-(1,3-benzothiazol-2-yl)phenyl]acetamide
Photuris pensylvanica
-
-
0.0019
resveratrol
Photinus pyralis
pH and temperature not specified in the publication
0.002
resveratrol
Photinus pyralis
pH and temperature not specified in the publication
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E270A
Amydetes vivianii
the mutation drastically decreases the spectral pH-sensitivity, and extends the activity profile above pH 9.0. These mutations also decrease the sensitivity to metals such as zinc, mercury and cadmium. The mutation may unwind a turn of the alpha-helix-10, indirectly increasing the interaction of the pH-sensor and other residues at the bottom of the luciferin binding site, stabilizing the green light emitting conformation
E270G
Amydetes vivianii
the mutation drastically decreases the spectral pH-sensitivity, and extends the activity profile above pH 9.0. These mutations also decrease the sensitivity to metals such as zinc, mercury and cadmium. The mutation may unwind a turn of the alpha-helix-10, indirectly increasing the interaction of the pH-sensor and other residues at the bottom of the luciferin binding site, stabilizing the green light emitting conformation
F227Y
the mutation causes dramatic redshift and temporal shift
F260L
the mutation results in a much less pH-sensitive enzyme displaying only a 10 nm redshift and broadening of the spectra at pH 6
I226A
the mutation causes dramatic redshift and temporal shift
E353Q/ins356R
emission of red and green light at pH 7.8, 20% less activity
E354K
emission of red and green light at pH 7.8, 26% higher activity
E354K/ins356R
emission of red and green light at pH 7.8, 20% higher activity
E354R
emission of red and green light at pH 7.8, 33% higher activity
E354R/ins356R
emission of red light at pH 7.8 compared to green emitted light by wild-type luciferase, 53% higher activity compared to wild-type luciferase
H245N
red- and green-emitting luciferase, increase in thermostability, about 25% decrease in relative activity
H431Y
red- and green-emitting luciferase, about 85% decrease in relative acitivity
L300E
specific activity is increased and Km-value is increased about 1.7fold compared with the wild-type enzyme
L300K
relative stability of mutant luciferase increases compared with native luciferase, mutation causes no effects on bioluminescence spectrum
L300R
relative stability of mutant luciferase increases compared with native luciferase, mutation causes no effects on bioluminescence spectrum, specific activity is increased as compared to wild-type enzyme
S284T
red-emitting luciferase, about 75% decrease in relative activity
S286N
red bioluminescence
F16L
lower pH-dependence of bioluminescence spectra, about 40% decrease in specific activity
F16L/A40S
bioluminescence spectra independent from pH in range of pH 6.0-7.8, about 80% decrease in specific activity
H433Y
-
higher affinity to monomethyloxyluciferin and dimethyloxyluciferin compared to the wild type enzyme
S118C
increased thermostability, about 30% increase in specific activity
Y35H
bioluminescence spectra independent from pH in range of pH 6.0-7.8, about 40% decrease in specific activity
Y35N
bioluminescence spectra independent from pH in range of pH 6.0-7.8, about 30% decrease in specific activity
E356R/V368A
-
mutant enzyme with significantly improved thermostability, more than 90% of the activity remains after incubation for 1 h at 45°C. Unlike the wild-type enzyme the mutant enzyme shows no change in the emission maximum of 568 nm even at pH 6.3
F227Y
Macrolampis sp2
-
the mutation results in a unique time-dependent shift from red to yellow-green
G228A
Macrolampis sp2
-
the mutation results in a large redshift
Y227A
Macrolampis sp2
-
the substitution results in a weak and unstable red mutant
A296C/A326C
-
specific activity 676% (compared to wild-type 100%), Km (ATP) decreased compared to wild-type, Km (D-luciferin) decreased compared to wild-type, optimal temperature 35° (wild-type 25°C), optimal pH 8.5 (wild-type pH 8), activity remains 54% at 40°C for 5 min (compared to wild-type 0%), t1/2: 40 min at 35°C (compared to wild-type 5 min)
A348V
-
Km-value for D-luciferin is 8.9fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 2fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 6.5fold higher compared to the Km-value of the wild-type enzyme
AC571TG
-
nonsense mutation
D436A
3.4fold increased activity compared to the wild type enzyme
D436E
50% activity compared to the wild type enzyme
D436N
50% activity compared to the wild type enzyme
D436S
2.2fold increased activity compared to the wild type enzyme
D436V
2% activity compared to the wild type enzyme
D474K
-
D476N mutation does not have any significant effect
D476N
-
D474K mutation destabilizes the protein. Flexibility analysis using dynamic quenching and limited proteolysis demonstrates that D474K mutation is much more flexible than wild-type
D476P
site-directed mutagenesis, the mutant shows decreased thermostability compared to the wild-type
DELTA438-550
-
the purified N-terminal domain 1-437 has luminescence activity by itself, and binds to substrates ATP and luciferin with reduced affinity
E311Q
site-directed mutagenesis, the mutant shows 65% specific activity compared to the wild-type
E345K/A215L
-
half-life at 37°C is 7.36 min, compared to 3.06 min for the wild-type enzyme
E345K/A215L/I232A/T214A
-
half-life at 37°C is 75.1 min, compared to 3.06 min for the wild-type enzyme
E345K/A215L/I232A/T214A/F295L
-
half-life at 37°C is 82.1 min, compared to 3.06 min for the wild-type enzyme
E345K/I232A/T214A
-
half-life at 37°C is 15.5 min, compared to 3.06 min for the wild-type enzyme
E345K/I232A/T214A/F295L/S420T
-
half-life at 37°C is 72.4 min, compared to 3.06 min for the wild-type enzyme
E345K/T214A
-
half-life at 37°C is 8.5 min, compared to 3.06 min for the wild-type enzyme
F14R
-
improved pH tolerance and stability up to 45°C, no decrease in specific activity relative to the recombinant wild type enzyme
F14R/L35Q/V182K/I232K/F465R
-
improved pH tolerance and stability up to 45°C, no decrease in specific activity relative to the recombinant wild type enzyme
F247A
-
Km-value for D-luciferin is 15.3fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 17.9fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 21.9fold higher compared to the Km-value of the wild-type enzyme
F247L
-
Km-value for D-luciferin is 8.3fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is nearly identical to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.4fold higher compared to the Km-value of the wild-type enzyme
F247Y
-
Km-value for D-luciferin is 1.2fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 128fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 2fold lower compared to the Km-value of the wild-type enzyme
F250T
37% specific activity at pH 7.8 compared to the wild type enzyme
F465R
-
improved pH tolerance and stability up to 45°C, no decrease in specific activity relative to the recombinant wild type enzyme
G246A/F250G
33% specific activity at pH 7.8 compared to the wild type enzyme
G246A/F250S
42% specific activity at pH 7.8 compared to the wild type enzyme
G246A/F250T
40% specific activity at pH 7.8 compared to the wild type enzyme
G315A
-
Km-value for D-luciferin is 13.3fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 625fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 7.5fold higher compared to the Km-value of the wild-type enzyme
G316A
-
Km-value for D-luciferin is 1.2fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 2.6fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.5fold lower compared to the Km-value of the wild-type enzyme
G341A
-
Km-value for D-luciferin is 4fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 625fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.3fold higher compared to the Km-value of the wild-type enzyme
G446I
turnover number is 8.4fold lower compared to wild-type value, KM-value for D-luciferin is 1.5fold lower compared to wild-type value, KM-value for MgATP2- is 2.2fold lower compared to wild-type value, the bioluminescence emission maximum is 554 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 5.1fold lower compared to wild-type value
H245A
-
Km-value for D-luciferin is identical to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 3fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.5fold higher compared to the Km-value of the wild-type enzyme
H245D
-
longest rise time known among single point mutants
H461D
relative specific activity is 57.6% as compared to wild-type enzyme. Mutation decreases ATP binding affinity, reduces the melting temperature of protein by around 25°C and shifts its optimum temperature of activity to 10°C
H489D
relative specific activity is 112% as compared to wild-type enzyme. Mutation introduces a new salt bridge between the C-terminal and N-terminal domains and increases protein rigidity but only slightly improves its thermal stability
H489K
relative specific activity is 115% as compared to wild-type enzyme. Mutation increases protein rigidity but only slightly improves its thermal stability
H489M
relative specific activity is 103% as compared to wild-type enzyme
H489P
site-directed mutagenesis, the mutant shows improved thermostability while maintaining its catalytic efficiency compared to that of wild-type luciferase, the overall rigidity and local rigidity of H489Pmutant are greatly strengthened
I147A
30% activity compared to the wild type enzyme
I147E
4% activity compared to the wild type enzyme
I147F
1.2fold increased activity compared to the wild type enzyme
I147G
3% activity compared to the wild type enzyme
I147K
4% activity compared to the wild type enzyme
I147L
4.7fold increased activity compared to the wild type enzyme
I147M
3.4fold increased activity compared to the wild type enzyme
I147Q
70% activity compared to the wild type enzyme
I147R
1% activity compared to the wild type enzyme
I147S
7% activity compared to the wild type enzyme
I147V
1.3fold increased activity compared to the wild type enzyme
I232K
-
improved pH tolerance and stability up to 45°C, no decrease in specific activity relative to the recombinant wild type enzyme
I232R
-
specific activity 75% (compared to wild-type 100%), Km (ATP) increased compared to wild-type, Km (D-luciferin) increased compared to wild-type, optimal temperature 25° (wild-type 25°C), optimal pH 8.5 (wild-type pH 8), activity remains 4% at 40°C for 5 min (compared to wild-type 0%), t1/2: 20 min at 35°C (compared to wild-type 5 min)
I232R/A296C/A326C
-
specific activity 358% (compared to wild-type 100%), Km (ATP) increased compared to wild-type, Km (D-luciferin) increased compared to wild-type, optimal temperature 35° (wild-type 25°C), optimal pH 8 (wild-type pH 8), activity remains 28% at 40°C for 5 min (compared to wild-type 0%), t1/2: 10 min at 35°C (compared to wild-type 5 min)
I351A
-
Km-value for D-luciferin is 5.7fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 1.5fold higher compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.8fold higher compared to the Km-value of the wild-type enzyme
ins356E
green and red emitting light at pH 7.8, at pH 5.5 red-emitting luciferase, 97% increase in specific activity
ins356K
green and red emitting light at pH 7.8, at pH 5.5 red-emitting luciferase, 18% decrease in specific activity
ins356Q
at pH 5.5 red-emitting luciferase, increase in thermostability, 6% decrease in specific activity
ins356R
green and red emitting light at pH 7.8, at pH 5.5 red-emitting luciferase, 12% decrease in specific activtiy
K329I
point mutation does not affect the orientation of critical residues in bioluminescence color determination. Thermostability and Km value for luciferin are decreased as compared to wild type enzyme. Intrinsic fluorescence and far-UV CD intensity in K329I mutant is decreased. Realative activity as compared to wild-type enzyme is 32%
K443A
turnover number is 2655 fold lower compared to wild-type value, KM-value for D-luciferin is 6.5fold lower compared to wild-type value, KM-value for MgATP2- is 3.3fold lower compared to wild-type value, the bioluminescence emission maximum is identical to the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 181fold lower compared to wild-type value
K443A/K529A
turnover number is 1063700fold lower compared to wild-type value, KM-value for D-luciferin is 4.5fold higher compared to wild-type value, KM-value for MgATP2- is 3.5fold higher compared to wild-type value, the bioluminescence emission maximum is 596 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 858fold lower compared to wild-type value
K445Q
turnover number is 1.4fold higher compared to wild-type value, KM-value for D-luciferin is 1.7fold lower compared to wild-type value, KM-value for MgATP2- is 2.3fold lower compared to wild-type value, the bioluminescence emission maximum is 556 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 1.7fold higher compared to wild-type value
L287I
-
orange light emitting mutant, mutation does not affect the structural integrity and/or folding of luciferase
L342A
-
Km-value for D-luciferin is 8.7fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 1.2fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 7.5fold higher compared to the Km-value of the wild-type enzyme
L35Q
-
improved pH tolerance and stability up to 45°C, no decrease in specific activity relative to the recombinant wild type enzyme
L530A
20% activity compared to the wild type enzyme
L530D
1% activity compared to the wild type enzyme
L530F
10% activity compared to the wild type enzyme
L530H
1.4fold increased activity compared to the wild type enzyme
L530I
shows wild type enzyme activity
L530K
3.2fold increased activity compared to the wild type enzyme
L530S
1% activity compared to the wild type enzyme
L530V
50% activity compared to the wild type enzyme
L530Y
2% activity compared to the wild type enzyme
N229T
site-directed mutagenesis, the mutant shows 63% specific activity compared to the wild-type
Q283R
-
red light emitting mutant, mutation does not affect the structural integrity and/or folding of luciferase
Q338P
-
about 50% decrease in specific activity compared to wild-type luciferase
Q448A
turnover number is 1.9fold lower compared to wild-type value, KM-value for D-luciferin is 2.5fold lower compared to wild-type value, KM-value for MgATP2- is 2.1fold higher compared to wild-type value, the bioluminescence emission maximum is 557 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 1.1fold lower compared to wild-type value
R213E
-
same activity like wild-type luciferase
R213K/T214N
site-directed mutagenesis, residues K213 and/or N214 are largely responsible for the 1.55fold increase in specific activity of the variant
R218A
-
Km-value for D-luciferin is 20fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 31.3fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 38.8fold higher compared to the Km-value of the wild-type enzyme
R218Q
site-directed mutagenesis, the mutant shows 125% specific activity compared to the wild-type
R330Q
point mutation does not affect the orientation of critical residues in bioluminescence color determination. Thermostability and Km value for luciferin are decreased as compared to wild type enzyme. Increase in tryptophan fluorescence intensity and secondary structure content for R330Q as compared with wild type. Realative activity as compared to wild-type enzyme is 23%
S184T
-
red-emitting luciferase with a bioluminescence maximum of 615 nm
S284G
-
red light emitting mutant, mutation does not affect the structural integrity and/or folding of luciferase
S293P
-
orange light emitting mutant, mutation does not affect the structural integrity and/or folding of luciferase
S307P/H489P
site-directed mutagenesis, the mutation is randomly chosen outside the flexible regions as a control. The mutant has decreased kinetic stability and enhanced thermodynamic stability compared to the wild-type
S347A
-
Km-value for D-luciferin is 11.3fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 4.2fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 2.2fold higher compared to the Km-value of the wild-type enzyme
S440P/S456Y
-
mutant shows improved specificity and reactivity for ATP compared to wild-type
S440R/S456A
-
mutant shows improved specificity and reactivity for ATP compared to wild-type
S440R/S456V
-
mutant shows improved specificity for ATP compared to wild-type
T214A/A215L/I232A/F295L/E345K
the mutant enzyme displays high thermostability, retaining about 60% activity after 120 min at 45°C. Although the mutant shows higher maximum activity at high D-luciferin concentrations, its activity at low D-luciferin concentrations (below 0.004 mM) lags behind that of the mutantI423L/D436G/L530R
T214A/A215L/I232A/F295L/E345K/I423L/D436G/L530R
the mutant enzyme exhibits both improved thermostability and brighter luminescence at low luciferin concentrations, it may be useful for reporter gene applications
T251A
-
Km-value for D-luciferin is 20.7fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 2.9fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 12.5fold higher compared to the Km-value of the wild-type enzyme
T343A
-
Km-value for D-luciferin is 6.6fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 125fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 5.4fold higher compared to the Km-value of the wild-type enzyme
V182K
-
improved pH tolerance and stability up to 45°C, no decrease in specific activity relative to the recombinant wild type enzyme
V241I
136% specific activity at pH 7.8 compared to the wild type enzyme
V241I/F250G
13% specific activity at pH 7.8 compared to the wild type enzyme
V241I/F250S
32% specific activity at pH 7.8 compared to the wild type enzyme
V241I/F250T
64% specific activity at pH 7.8 compared to the wild type enzyme
V241I/G246A/F250S
73% specific activity at pH 7.8 compared to the wild type enzyme
V241I/G246A/F250T
83% specific activity at pH 7.8 compared to the wild type enzyme
Y255F
site-directed mutagenesis, the mutant shows 71% specific activity compared to the wild-type
F255Y
site-directed mutagenesis, the single change Y255F is necessary and sufficient for a 13 nm redshift in bioluminescence
Y227A
mutant shows enzymatic behaviour similar to the wild type enzyme
G228A
the mutation results in a large redshift
Y227A
the mutation causes dramatic red- and time-dependent shifts
L260F
-
mutation results in a 20 nm redshift without affecting pH-insensitivity
V227A
-
mutant displays a small redshift
V227F
-
mutation results in a 60 nm redshift
V227I
-
mutant displays a small redshift
V227S
-
mutant displays a small redshift
A243G
-
bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 599 nm compared to 549 nm for the wild-type enzyme, bioluminescence emission maxima with 5,5-dimethyl-luciferyl-O-adenosine monophosphate are 610 nm and 557 nm compared to 624 nm for the wild-type enzyme
S247F
-
bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 597 nm compared to 549 nm for the wild-type enzyme, bioluminescence emission maximum with 5,5-dimethyl-luciferyl-O-adenosine monophosphate is 612 nm compared to 624 nm for the wild-type enzyme
D436G
8.5fold increased activity compared to the wild type enzyme
D436G
exhibits 8.5fold higher luciferase activity than the wild type enzyme
D436G
shows 8.5fold increase in luminescence intensity
F250G
-
Km-value for D-luciferin is neraly identical to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 9.6fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is nearly identical to the Km-value of the wild-type enzyme
F250G
23% specific activity at pH 7.8 compared to the wild type enzyme
F250S
-
bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 546 nm compared to 552 nm for the wild-type enzyme, bioluminescence emission maxima with 5,5-dimethyl-luciferyl-O-adenosine monophosphate are 631 nm and 552 nm compared to 560 nm for the wild-type enzyme
F250S
-
Km-value for D-luciferin is 1.5fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 3.5fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 1.2fold lower compared to the Km-value of the wild-type enzyme
F250S
49% specific activity at pH 7.8 compared to the wild type enzyme
G246A
-
bioluminescence emission maximum with luciferyl-O-adenosine monophosphate is 548 nm compared to 552 nm for the wild-type enzyme, bioluminescence emission maximum with 5,5-dimethyl-luciferyl-O-adenosine monophosphate is 578 nm compared to 560 nm for the wild-type enzyme
G246A
-
Km-value for D-luciferin is 3.6fold lower compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 2.1fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 5.5fold lower compared to the Km-value of the wild-type enzyme
G246A
104% specific activity at pH 7.8 compared to the wild type enzyme
I423L
exhibits 4.7fold higher luciferase activity than the wild type enzyme
I423L
shows 4.7fold increase in luminescence intensity
I423L/D436G/L530R
exhibits 12.5fold higher luciferase activity than the wild type enzyme
I423L/D436G/L530R
combining the mutations results in a combined mutant luciferase with higher luminescence intensity than any of the single mutant luciferases, generates more than 12.5fold higher luminescence intensity than the wild-type enzyme. The combined mutant luciferase detects ATP at 10-18 mol, whereas wild-type luciferase is unable to detect below 10-17 mol ATP
I423L/D436G/L530R
the mutant shows a lower apparent Km value of 0.00076 mM than that of the wild-type enzyme
K529A
-
Km-value for D-luciferin is 15.3fold higher compared to the Km-value of the wild-type enzyme, the turnover-number for D-luciferin is 1250fold lower compared to the turnover-number of the wild-type enzyme, the Km-value for MgATP2- is 7.5fold higher compared to the Km-value of the wild-type enzyme
K529A
turnover number is 668fold lower compared to wild-type value, KM-value for D-luciferin is 15.3fold higher compared to wild-type value, KM-value for MgATP2- is 7.5fold higher compared to wild-type value, the bioluminescence emission maximum is 562 nm, compared to 558 nm for the wild-type value. The ratio of turnover-number to KM-value for D-luciferyl-O-adenosine monophosphate is 3.5fold lower compared to wild-type value
K529A
-
similar rise time compared to wild type enzyme
L530R
5.1fold increased activity compared to the wild type enzyme
L530R
exhibits 5.1fold higher luciferase activity than the wild type enzyme
L530R
shows 5.1fold increase in luminescence intensity
R213M
-
3fold activity compared to wild-type luciferase
R213M
-
Cm (M): 1.8 (wild-type: 2.4), T1/2 (min): 19.5 (wild-type: 19.5), Tm (°C): 46.5 (wild-type: 46.5), activation energy (kcal/mol): 2.59 (wild-type: 6.51), [urea]50% (M): 2.86 (wild-type: 1.35)
R337Q
-
only 60% relative specific activity compared to wild-type luciferase, higher light stability, most stable luciferase mutant against trypsin hydrolysis at 23 and 37°C
R337Q
-
Cm (M): 1.7 (wild-type: 2.4), T1/2 (min): 22.1 (wild-type: 19.5), Tm (°C): 50.7 (wild-type: 46.5), activation energy (kcal/mol): 3.39 (wild-type: 6.51), [urea]50% (M): 2.18 (wild-type: 1.35)
R337Q
site-directed mutagenesis, the mutant shows 26% specific activity compared to the wild-type
S284T
-
red-emitting mutant, about 75% decrease of activitiy in vitro, in vivo more efficient light production
S284T
site-directed mutagenesis, a red-emitting mutant variant, the mutant shows 25% specific activity compared to the wild-type
additional information
construction of a chimeric enzyme luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme shows 2fold enhanced activity and 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. Further engineering to enhance thermal and pH stability produces a different luciferase called PLG2, that shows 4.4fold enhanced activity and 2.2fold greater bioluminescence quantum yield compared to the wild-type. Five amino acid changes based on Luciola italica are the main determinants of the improved bioluminescence properties
additional information
-
construction of a chimeric enzyme luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme shows 2fold enhanced activity and 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. Further engineering to enhance thermal and pH stability produces a different luciferase called PLG2, that shows 4.4fold enhanced activity and 2.2fold greater bioluminescence quantum yield compared to the wild-type. Five amino acid changes based on Luciola italica are the main determinants of the improved bioluminescence properties
additional information
construction of a chimeric enzyme PpyLit that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme PpyLit shows 1.8fold enhanced flash-height specific activity, 2.0fold enhanced integration-based specific activity, 2.9fold enhanced catalytic efficiency (kcat/Km), and a 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. A chimeric enzyme with enhanced catalytic properties that are not simply the sum of the contributions of the two luciferases
additional information
-
construction of a chimeric enzyme PpyLit that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme PpyLit shows 1.8fold enhanced flash-height specific activity, 2.0fold enhanced integration-based specific activity, 2.9fold enhanced catalytic efficiency (kcat/Km), and a 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. A chimeric enzyme with enhanced catalytic properties that are not simply the sum of the contributions of the two luciferases
additional information
a chimeric protein with the N-terminal domain of firefly luciferase and the C-terminal domain of the firefly luciferase homolog from Drosophila melanogaster CG6178 shows approximately 4% of the activity of wild type firefly luciferase
additional information
-
a chimeric protein with the N-terminal domain of firefly luciferase and the C-terminal domain of the firefly luciferase homolog from Drosophila melanogaster CG6178 shows approximately 4% of the activity of wild type firefly luciferase
additional information
-
mutants with changes in V241I, G246A, and F250S show emission maximum blue-shifted to 549 nm
additional information
-
10fold higher luminescence intensity of mutant enzyme luciferase FM compared to wild-type luciferase
additional information
chimeric protein with fatty acyl-CoA synthetase, EC 6.2.1.3, 4% of luminescence activity from wild-tpe luciferase activity
additional information
concept of tumor monitoring using dual luciferases, construction of the expression vector, and evaluation of tumor monitoring systems using dual luciferases from Cypridina noctiluca and firefly Photinus pyralis, overview. The enzymes are expressed in human breast cancercells MDA-MB-231, followed by inoculatin of the MDA-MB-231/FIC cell suspension subcutaneously into the back of 6-week-old male nude mice lacking T-cell function (BALB/cAJcl-nu/nu). The expressed CLuc is secreted into the blood from the cells and circulates in the living body. The blood containing CLuc can be drawn by using glass micro-hematocrit capillary tubes or a syringe
additional information
construction of a chimeric enzyme luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme shows 2fold enhanced activity and 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. Further engineering to enhance thermal and pH stability produces a different luciferase called PLG2, that shows 4.4fold enhanced activity and 2.2fold greater bioluminescence quantum yield compared to the wild-type. Five amino acid changes based on Luciola italica are the main determinants of the improved bioluminescence properties, comparison to the Photinus pyralis luciferase wild-type, overview
additional information
-
construction of a chimeric enzyme luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme shows 2fold enhanced activity and 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. Further engineering to enhance thermal and pH stability produces a different luciferase called PLG2, that shows 4.4fold enhanced activity and 2.2fold greater bioluminescence quantum yield compared to the wild-type. Five amino acid changes based on Luciola italica are the main determinants of the improved bioluminescence properties, comparison to the Photinus pyralis luciferase wild-type, overview
additional information
construction of a chimeric enzyme PpyLit that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme PpyLit shows 1.8fold enhanced flash-height specific activity, 2.0fold enhanced integration-based specific activity, 2.9fold enhanced catalytic efficiency (kcat/Km), and a 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. A chimeric enzyme with enhanced catalytic properties that are not simply the sum of the contributions of the two luciferases
additional information
-
construction of a chimeric enzyme PpyLit that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase, the recombinant chimeric enzyme PpyLit shows 1.8fold enhanced flash-height specific activity, 2.0fold enhanced integration-based specific activity, 2.9fold enhanced catalytic efficiency (kcat/Km), and a 1.4fold greater bioluminescence quantum yield compared to the wild-type Photinus pyralis luciferase. A chimeric enzyme with enhanced catalytic properties that are not simply the sum of the contributions of the two luciferases
additional information
enzyme activity and structural stability increases in presence of magnetic magnetite (lambda-Fe2O3) nanoparticles supported ionic liquids. The effect of ingredients which are used is not considerable on Km value of luciferase for ATP and also Km value for luciferin, synthesis and evaluation, overview. The use of ionic liquids supported on magnetic nanoparticles improves kinetic and structural properties of firefly luciferase using bioluminescence assay, fluorescence spectroscopy, and circular dichroism
additional information
-
enzyme activity and structural stability increases in presence of magnetic magnetite (lambda-Fe2O3) nanoparticles supported ionic liquids. The effect of ingredients which are used is not considerable on Km value of luciferase for ATP and also Km value for luciferin, synthesis and evaluation, overview. The use of ionic liquids supported on magnetic nanoparticles improves kinetic and structural properties of firefly luciferase using bioluminescence assay, fluorescence spectroscopy, and circular dichroism
additional information
firefly luciferase from Photinus pyralis is cyclized in vivo by fusing SpyCatcher at the N-terminus and SpyTag at the C-terminus. SpyTag can spontaneously form a covalent isopeptide bond with its protein partner Spy-Catcher. Circular LUC is more thermostable at 25-55°C and alkali-tolerant than the wild-type, without compromising the specific activity. Preparation of an N-terminally and C-terminally shortened form of the SpyCatcher protein and enzyme cyclization using this truncated form leads to even more thermostability of the construct than the full-length SpyCatcher form, method optimization
additional information
-
firefly luciferase from Photinus pyralis is cyclized in vivo by fusing SpyCatcher at the N-terminus and SpyTag at the C-terminus. SpyTag can spontaneously form a covalent isopeptide bond with its protein partner Spy-Catcher. Circular LUC is more thermostable at 25-55°C and alkali-tolerant than the wild-type, without compromising the specific activity. Preparation of an N-terminally and C-terminally shortened form of the SpyCatcher protein and enzyme cyclization using this truncated form leads to even more thermostability of the construct than the full-length SpyCatcher form, method optimization
additional information
for large scale enzyme production, a simple production procedure is established using plant cell cultures. The plant cell culture tobacco BY-2 efficiently secretes luciferase, which is easily purified using a simple one-step ion-exchange chromatography method. The production yield is 20-30 mg of luciferase per liter of culture medium. The method offers a cost-effective production for Cypridina luciferase
additional information
Photinus scintillans luciferases PsnWT is significantly more resistant to long wavelength emission shifts than Photinus pyralis luciferase PpyWT at pH 7.0 and pH 6.0
additional information
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Photinus scintillans luciferases PsnWT is significantly more resistant to long wavelength emission shifts than Photinus pyralis luciferase PpyWT at pH 7.0 and pH 6.0
additional information
Photinus scintillans luciferases PsnWT is significantly more resistant to long wavelength emission shifts than Photinus pyralis luciferase PpyWT at pH 7.0 and pH 6.0
additional information
-
Photinus scintillans luciferases PsnWT is significantly more resistant to long wavelength emission shifts than Photinus pyralis luciferase PpyWT at pH 7.0 and pH 6.0
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15 - 40
at 35°C native luciferase completely inactive, mutant H245N still 80% residual activity, mutant S284T and H431Y about 20% residual activity
15 - 45
-
when native and mutants are incubated 5 min at temperatures ranging from 15 to 45°C, D474K mutant is inactivated faster than native and D476N at all temperatures
16.7
Tm value of recombinant wild-type LUC
20
-
after 20 min only 5% activity in the absence of ionic liquids but less than 1% in the presence of [1,1,3,3-tetramethylguanidine][lactate] and [1,1,3,3-tetramethylguanidine][propionate]
23
-
stability remains constant upon 120 min
25
t1/2: 17 min (wild-type enzyme), 9.5 min (mutant enzyme H461D), 12.6 min (mutant enzyme H489K), 20.2 min (mutant enzyme H489D) and 24.4 min (mutant enzyme H489M)
35 - 45
free enzyme shows 65% remaning activity after 10 min at 35°C, inactivation after 4 min at 35°C, inactivation at 45°C
37.4
T50 for recombinant wild-type LUC
40.3
T1/2 value of recombinant cyclized LUC
47.5
T50 for recombinant cyclized LUC
49.2
T50 value of recombinant cyclized LUC with truncated Spy-Catcher cyclization protein
50
-
half-life: 3 h, isoenzyme AL2
51.4
T1/2 value of recombinant cyclized LUC with truncated Spy-Catcher cyclization protein
53.5
Tm value of recombinant wild-type LUC
60
-
half-life: 10 min, isoenzyme AL2
70.2
Tm value of recombinant cyclized LUC
73.1
Tm value of recombinant cyclized LUC with truncated Spy-Catcher cyclization protein
25 - 45
activity starts to decrease above 25°C and is almost completely lost at 45°C
25 - 45
activity starts to decrease above 25°C and is almost completely lost at 45°C
30
-
after 20 min 10% remaining activity, native enzyme
30
-
after 20 min more less than 1% remaining activity in the presence of [1,1,3,3-tetramethylguanidine][propionate]
30
-
after 20 min more than 10% remaining activity in the presence of [1,1,3,3-tetramethylguanidine][lactate]
30
-
T1/2 (min): 16.2 (wild-type), 19.5 (mutant R213M), 22.1 (mutant R337Q)
30
t1/2: 10.5 min (wild-type enzyme), 6.9 min (mutant enzyme H461D), 8.3 min (mutant enzyme H489K), 11.1 min (mutant enzyme H489D) and 9.5 min (mutant enzyme H489M)
32
mutant E354R, E354K, E354R/ins356Arg with greater thermostability than wild-type luciferase
32
-
after 20 min at 32°C wild-type and mutant D476N retain 24% original activity whereas mutant D474K shows only 2% remaining activity
35
thermostability of recombinant wild-type and mutant enzymes, overview
35
-
about 70% loss of activity within 10 min, no residual activity after 60 min, in presence of osmolytes higher residual activity after 60 min: 90% with 1.5 M sucrose, 50% with 1.5 M sorbitol, 35% with 1.5 M proline
35
-
T1/2 results show that half-lives (t1/2) of wild-type, mutant A296C/A326C, mutant A296C/A326C/I232R and mutant I232R are 5, 40, 10 and 20 min at 35°C respectively
35
t1/2: 6.1 min (wild-type enzyme), 3.7 min (mutant enzyme H461D), 6.4 min (mutant enzyme H489K), 6.5 min (mutant enzyme H489D) and 5.7 min (mutant enzyme H489M)
37
-
half-life: 48 h, isoenzyme AL2. half-life: 1 h, isoenzyme AL1
37
-
half-life: 3.06 min for wild-type enzyme,8.5 min for mutant enzyme E345K/T214A, 15.5 min for E345K/I232A/T214A, 7.36 min for E345K/A215L, 72.4 min for E345K/I232A/T214A/F295L/S420T, 82.1 min for E345K/A215L/I232A/T214A/F295L, 75.1 min for E345K/A215L/I232A/T214A
37
-
high loss of activity in less than 10 min
37
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 47 min
37
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 240 min
37
4 h, 90% resiudal activity, 24 h, 70% residual activity, respectively, for engineered commercial enzyme. Wild-type enzyme loses 80% of initial activity within 39 min
37
10 min, complete loss of activity
40
-
at 40°C for 45 min the activity of the enzyme decreased to less than 1% of control
40
immobilized enzyme forms are stable for 1 min at 40°C and then lose their activities
40
complete inactivation, mutant ins356Q still 20% residual activity
40
-
thermal stability experiments of mutant A296C/A326C, mutant A296C/A326C/I232R and mutant I232R shows that their original activity remains approximately 54%, 28%, and 4% after incubation at 40°C for 5 min, respectively (compared to wild-type 0%)
42
50% decrease in activity after 6.9 min for wild-type luciferase, for mutant S118C after 13.4 min
42
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 50 s
42
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 61 s
45
-
1 h, less than 10% loss of activity mutant enzyme E356R/V368A
45
-
mutant enzymes F14R, L35Q, V182K, I232K and F465R are stable up to 45°C
45
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 25 s
45
the mutant enzyme T214A/A215L/I232A/F295L/E345K displays high thermostability, retaining about 60% activity after 120 min at 45°C
45
thermal inactivation of purified recombinant wild-type enzyme at pH 7.4 after 40 s
55
complete inactivation
additional information
-
10 min at 50°C decreases activity by 90%
additional information
-
a chimeric protein derived from Photinus pyralis and Luciola cruciata luciferases is more stable than the wild type enzyme, retaining 75% of the activity after 10 min at 50°C
additional information
-
higher stability in frozen state than in refrigerated
additional information
-
no activity at 40°C
additional information
thermal stability and activity at 35°C of the enzyme in presence of magnetic magnetite nanoparticles supported ionic liquids is increased compared to the free enzyme, overview
additional information
-
thermal stability and activity at 35°C of the enzyme in presence of magnetic magnetite nanoparticles supported ionic liquids is increased compared to the free enzyme, overview
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a chimeric protein derived from Photinus pyralis and Luciola cruciata luciferases expressed in Escherichia coli
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cloning of the cDNA encoding the destabilized enzyme into an adenoviral expression plasmid and transfection of Vero, Hep-2, Chang, A-549, COS-1, and HeLa cells, luciferase expression is linear with respect to viral multiplicity of infection, protein synthesis inhibiting drugs, e.g. shiga toxins of Escherichia coli, diphtheria toxin, Pseudomonas exotoxin A and the plant toxin ricin A, and cycloheximide, reduce bioluminescence respresenting the antiviral activity
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complete nucleotide sequence, expression in mammalian cells
-
Escherichia coli BL21 (DE3)
expressed in Candida albicans strain CAI4
-
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Escherichia coli JM109 cells and Bacillus subtilis strain NBRC13719
expressed in Escherichia coli strain BL21
expressed in Escherichia coli strain HMS174(DE3)
expressed in Escherichia coli strain JM109
expressed in Escherichia coli strain LE 392
-
expressed in Escherichia coli strains XL1-Blue and BL21
expressed in Escherichia coli Top10 cells
-
expressed in Escherichia coli XL1-Blue cells
expressed in Escherichia coli XL10-Gold cells
-
expressed in Saccharomyces cerevisiae
-
expression in Drosophila
-
expression in Escherichia coli
expression in Escherichia coli BL21
expression in Escherichia coli BL21 and DH5alpha, transfection in CHO-cells
-
expression in Escherichia coli BL21 and XL1blue
expression in Escherichia coli BL21 Star (DE3)
expression in Escherichia coli BL21-DE3 cells
Amydetes vivianii
expression in Escherichia coli, transfection in human glioma cells and in quadriceps muscles of mice
-
expression in HEK-293 cells or Grip-Tite 293 MSR cells
-
expression in HEK-293T cells
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expression in L16 derived from CV-1 monkey kidney cells
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expression in mouse cells
-
expression in PC3 cells
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expression in Spodoptera frugiperda clone 9-cells, expression in insect cells using a baculovirus vector
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expression in transfected Leishmania amazonensis strain LV79 amastigotes, transfection by electroporation
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expression of a polyhystidine tagged enzyme in Trichoplusia
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expression of a recombinant enzyme containing a protein kinase A recognition site
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expression of a recombinant luciferase-ubiquitin enzyme in Saccharomyces cerevisiae
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expression of the wild type and three mutants in Escherichia coli
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firefly lantern cDNA library
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gene expression in vegetative and symbiotic Rhizobium melioti and other gram-negative bacteria
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gene luc, DNA and amino acid sequence determination and analysis, sequence comparisons of Photinus pyralis and Photinus scintillans luciferases, the single conservative amino acid change tyrosine to phenylalanine at position 255 accounts for the entire emission color difference, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) pLysS, recombinant Luc contains the N-terminal peptide GlyProLeuGlySer-
mutant enzymes,R218A, H245A, G246A, F247A, F247L, F247Y, F250G, F250S, T251A, G315A, G316A, G341A, L342A, T343A, S347A, A348V, I351A and K529A
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Nn-terminal domain, expression in Escherichia coli
-
overexpressed in Escherichia coli BL-21
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recombinant coexpression of the luciferase with fused cyclization proteins SpyCatcher at the N-terminus and SpyTag at the C-terminus (pyCatcher-LUC-SpyTag) in Escherichia coli strain BL21(DE3)
recombinant expression from vector p35SHSPG in Nicotiana benthamiana BY-2 cells with intracellular enzyme localization, recombinant expression of the enzyme in Arabidopsis thaliana roots with enzyme localization around the nucleus, outside of the central vacuole and in the protoplasm
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of the chimeric mutant luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase in HEK-293 cells and in Escherichia coli strain BL21(DE3)pLysS
wild-type and mutant enzymes are expressed as GST-fusion proteins
wild-type and mutant enzymes expressed as glutathione-S-transferase-fusion proteins containing the additional N-terminal peptide Gly-Pro-Leu-Gly-SER, which remains after PreScission protease cleavage from GST, expression in Escherichia coli
-
-
expressed in Escherichia coli
-
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli strain BL21
-
expressed in Escherichia coli strain BL21
expressed in Escherichia coli strains XL1-Blue and BL21
expressed in Escherichia coli strains XL1-Blue and BL21
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli BL21
-
expression in Escherichia coli BL21
expression in Escherichia coli BL21
-
expression in Escherichia coli BL21
expression in Escherichia coli BL21
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gene luc, DNA and amino acid sequence determination and analysis, sequence comparisons of Photinus pyralis and Photinus scintillans luciferases, the single conservative amino acid change tyrosine to phenylalanine at position 255 accounts for the entire emission color difference, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) pLysS, recombinant Luc contains the N-terminal peptide GlyProLeuGlySer-
gene luc, DNA and amino acid sequence determination and analysis, sequence comparisons of Photinus pyralis and Photinus scintillans luciferases, the single conservative amino acid change tyrosine to phenylalanine at position 255 accounts for the entire emission color difference, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) pLysS, recombinant Luc contains the N-terminal peptide GlyProLeuGlySer-
recombinant expression of the chimeric mutant luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase in HEK-293 cells and in Escherichia coli strain BL21(DE3)pLysS
recombinant expression of the chimeric mutant luc2 that contains the N-domain of Photinus pyralis luciferase joined to the C-domain of Luciola italica luciferase in HEK-293 cells and in Escherichia coli strain BL21(DE3)pLysS
wild-type and mutant enzymes are expressed as GST-fusion proteins
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wild-type and mutant enzymes are expressed as GST-fusion proteins
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industry
the enzyme is widely used in academia and industry due to its excellent sensitivity and dynamic range, and its ease of use
analysis
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luminescence-based assays for ATP measurement in clinical chemistry and hygiene monitoring
analysis
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development of a quantitative and highly sensitive luciferase-based assay for bacterial toxins, overview
analysis
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expression of bioluminescent luciferase can be used for rapid and high throughput screening of drugs, e.g. quinolines, acting on Leishmania amastigote-harbouring macrophages and for quantitative real-time monitoring of parasitism features in living mice, overview
analysis
analytical assay of metabolites like ATP, CoA, pyrophosphate, AMP
analysis
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optical bioluminescence-based molecular imaging
analysis
Cypridina noctiluca luciferase is utilized for biochemical and molecular biological applications, including bioluminescent enzyme immunoassays, far-red luminescence imaging, and high-throughput reporter assays
analysis
the secreted Cypridina luciferase (CLuc) is used as an ex vivo indicator to continuously monitor tumor progression. On the other hand, the non-secreted firefly luciferase is used as an in vivo indicator to analyze the spatial distribution of the tumor at suitable time points indicated by CLuc. Tumor monitoring systems using dual luciferases are available, allowing long-term bioluminescence imaging under minimal stress for the experimental animals, e.g. BALB/cAJcl-nu/nu mice
analysis
an engineered, commercial thermostable luciferase is suitable for real-time monitoring of ATP release by bacteria, both in broth culture and on agar surfaces, which allows for the estimation of viable cell number by relating luminescence onset time to initial cell concentration. The method is able to rapidly detect the effect of antibiotics on bacterial cultures
analysis
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luciferase-based determination of ATP/NAD(H) pools in combination with a microplate reader and the marine model bacterium Phaeobacter inhibens. Grey multiwell plates best balance sensitivity and crosstalk, and optimal incubation times are 5 min and 30 min for the ATP and NAD(H) assay, respectively, together allowing limits of detection of 0.042, 0.470 and 0.710 nM for ATP, NAD+, and NADH, respectively
analysis
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luciferase-based determination of ATP/NAD(H) pools in combination with a microplate reader and the marine model bacterium Phaeobacter inhibens. Grey multiwell plates best balance sensitivity and crosstalk, and optimal incubation times are 5 min and 30 min for the ATP and NAD(H) assay, respectively, together allowing limits of detection of 0.042, 0.470 and 0.710 nM for ATP, NAD+, and NADH, respectively
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biotechnology
imaging technology
biotechnology
molecular biology studies with luciferase as reproter gene, bioimaging
biotechnology
extensive and advantageous application of this enzyme in biotechnology is restricted due to its low thermal stability
medicine
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luciferase gene is a useful reporter gene in vivo, allowing noninvasive imaging of tumor growth, metastasis, gene transfer, drug treatment, and gene expression. The use of thermostabilized luciferases may allow monitoring of micro-metastses and the early stages of tumor growth
medicine
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observing tumours
medicine
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use in endotoxin detection method
molecular biology
Cypridina noctiluca luciferase is utilized for biochemical and molecular biological applications, including bioluminescent enzyme immunoassays, far-red luminescence imaging, and high-throughput reporter assays
molecular biology
firefly luciferase is widely used in molecular biology and bioanalytical systems as a reporter molecule due to the high quantum yield of the bioluminescence, availability of stable mutant forms of the enzyme with prescribed spectral characteristics and abundance of bacterial expression systems suitable for production of recombinant proteins in limitless quantities. Fusion proteins of luciferase are described with biotin-binding domain and treptavidin, with proteins A and G, antibodies, with DNA- and RNA-binding proteins, as well as fusion proteins designed for BRET systems. The firefly luciferase-based fusion proteins are represented as an effective tool for the development of different bioanalytical systems such as (1) systems in which luciferase is attached to the surface of the target and the bioluminescence signal is detected from the specific complexes formed, (2) BRET-based systems, in which the specific interaction induces changes in the bioluminescence spectrum, and (3) systems that use modified or split luciferases, in which the luciferase activity changes under the action of the analyte. All these systems have wide application in biochemical analysis of physiologically important compounds, for the detection of pathogenic bacteria and viruses, for evaluation of protein-protein interactions, assaying of metabolites involved in cell communication and cell signaling
molecular biology
firefly luciferase is widely used in molecular biology and bioanalytical systems as a reporter molecule due to the high quantum yield of the bioluminescence, availability of stable mutant forms of the enzyme with prescribed spectral characteristics and abundance of bacterial expression systems suitable for production of recombinant proteins in limitless quantities. Fusion proteins of luciferase are described with biotin-binding domain and treptavidin, with proteins A and G, antibodies, with DNA- and RNA-binding proteins, as well as fusion proteins designed for BRET systems. The firefly luciferase-based fusion proteins are represented as an effective tool for the development of different bioanalytical systems such as (1) systems in which luciferase is attached to the surface of the target and the bioluminescence signal is detected from the specific complexes formed, (2) BRET-based systems, in which the specific interaction induces changes in the bioluminescence spectrum, and (3) systems that use modified or split luciferases, in which the luciferase activity changes under the action of the analyte. All these systems have wide application in biochemical analysis of physiologically important compounds, for the detection of pathogenic bacteria and viruses, for evaluation of protein-protein interactions, assaying of metabolites involved in cell communication and cell signaling
molecular biology
firefly luciferase is widely used in molecular biology and bioanalytical systems as a reporter molecule due to the high quantum yield of the bioluminescence, availability of stable mutant forms of the enzyme with prescribed spectral characteristics and abundance of bacterial expression systems suitable for production of recombinant proteins in limitless quantities. Fusion proteins of luciferase are described with biotin-binding domain and treptavidin, with proteins A and G, antibodies, with DNA- and RNA-binding proteins, as well as fusion proteins designed for BRET systems. The firefly luciferase-based fusion proteins are represented as an effective tool for the development of different bioanalytical systems such as (1) systems in which luciferase is attached to the surface of the target and the bioluminescence signal is detected from the specific complexes formed, (2) BRET-based systems, in which the specific interaction induces changes in the bioluminescence spectrum, and (3) systems that use modified or split luciferases, in which the luciferase activity changes under the action of the analyte. All these systems have wide application in biochemical analysis of physiologically important compounds, for the detection of pathogenic bacteria and viruses, for evaluation of protein-protein interactions, assaying of metabolites involved in cell communication and cell signaling
molecular biology
Ppy luciferase can been used extensively as a reporter gene in living cells and organisms. Some biological applications are limited by the low stability of the luciferase and limited intracellular luciferin concentration. The mutant enzyme T214A/A215L/I232A/F295L/E345K/I423L/D436G/L530R exhibits both improved thermostability and brighter luminescence at low luciferin concentrations, it may be useful for reporter gene applications
molecular biology
the enzyme is a powerful tool for molecular and cellular biology, and popular in high-throughput screening and drug discovery
additional information
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the combined mutant luciferase, which has high luminescence intensity, will be useful for detecting bacteria with high sensitivity in production safety tests
additional information
the combined mutant luciferase, which has high luminescence intensity, will be useful for detecting bacteria with high sensitivity in production safety tests