1.14.14.3: bacterial luciferase
This is an abbreviated version!
For detailed information about bacterial luciferase, go to the full flat file.
Word Map on EC 1.14.14.3
-
1.14.14.3
-
metastasis
-
transwell
-
bioluminescence
-
chromatin
-
lncrnas
-
sponge
-
tumorigenesis
-
endothelial
-
3\'utr
-
transactivation
-
firefly
-
3'-untranslated
-
necrosis
-
agonist
-
tnf
-
prostate
-
estrogen
-
sp1
-
luminescence
-
nude
-
nf-kappab
-
5'-flanking
-
epithelial-mesenchymal
-
co-transfection
-
cyclin
-
glioma
-
nsclc
-
emsas
-
ovarian
-
carcinogenesis
-
mapks
-
pull-down
-
hypoxia-inducible
-
osteoblast
-
erk
-
non-small
-
bcl-2
-
adenovirus
-
osteosarcoma
-
chemoresistance
-
stat3
-
pten
-
c-jun
-
tunel
-
e-cadherin
-
cardiomyocytes
-
transcription-quantitative
-
runx2
-
osteogenic
-
homeobox
-
biotechnology
-
agriculture
-
diagnostics
-
medicine
-
molecular biology
-
analysis
- 1.14.14.3
- metastasis
-
transwell
-
bioluminescence
- chromatin
- lncrnas
- sponge
- tumorigenesis
- endothelial
-
3\'utr
-
transactivation
- firefly
-
3'-untranslated
- necrosis
- agonist
- tnf
- prostate
- estrogen
- sp1
-
luminescence
-
nude
- nf-kappab
-
5'-flanking
-
epithelial-mesenchymal
-
co-transfection
- cyclin
- glioma
-
nsclc
-
emsas
- ovarian
- carcinogenesis
- mapks
-
pull-down
-
hypoxia-inducible
- osteoblast
- erk
-
non-small
- bcl-2
- adenovirus
- osteosarcoma
-
chemoresistance
- stat3
- pten
- c-jun
-
tunel
- e-cadherin
- cardiomyocytes
-
transcription-quantitative
- runx2
-
osteogenic
-
homeobox
- biotechnology
- agriculture
- diagnostics
- medicine
- molecular biology
- analysis
Reaction
Synonyms
4a-hydroperoxy-4a,5-dihydroFMN intermediate luciferase, aldehyde monooxygenase, alkanal monooxygenase (FMN), bacterial luciferase, COB, Gluc luciferase, HFOOH, luciferase, Lux, LuxA, LuxAB, LuxB, LuxCDABE, LuxF, Vibrio fischeri luciferase, Vibrio harveyi luciferase
ECTree
1.14.14.3 bacterial luciferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.14.14.3 - bacterial luciferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-N,N-(dimethyl)aminonaphthalene-9-N-(11-aldehydedodecyl)-1,8-dicarboximide + FMNH2 + O2
? + FMN + H2O + hnu
-
-
-
-
?
4-N,N-(dimethyl)aminonaphthalene-9-N-(9-aldehyde-decyl)-1,8-dicarboximide + FMNH2 + O2
? + FMN + H2O + hnu
-
-
-
-
?
4-N-(11-aldehyde-dodecyl)-7-N,N-dimethylsulfonic-2,1,3-benzoxadiazole + FMNH2 + O2
? + FMN + H2O + hnu
-
-
-
-
?
4-N-(9-aldehyde-decyl)-7-N,N-dimethylsulfonic-2,1,3-benzoxadiazole + FMNH2 + O2
? + FMN + H2O + hnu
-
-
-
-
?
coelenterazine + FMNH2 + O2
CO2 + coelenteramide + FMN + light + H2O
-
an imidazolopyrazine derivative
-
-
ir
decanal + riboflavin + O2
?
-
riboflavin is a very poor substrate for bacterial luciferase
-
-
?
myristic aldehyde + FMNH + O2
myristic acid + FMN + H2O + light
-
-
-
-
?
(E)-dec-2-enal + FMNH2 + O2
(E)-dec-2-enoate + FMN + H2O + hn
-
-
-
-
?
(E)-dec-2-enal + FMNH2 + O2
(E)-dec-2-enoate + FMN + H2O + hn
-
-
-
-
?
(E)-dec-2-enal + FMNH2 + O2
(E)-dec-2-enoate + FMN + H2O + hn
-
-
-
-
?
(E)-dodec-2-enal + FMNH2 + O2
(E)-dodec-2-enoate + FMN + H2O + hn
-
-
-
-
?
(E)-dodec-2-enal + FMNH2 + O2
(E)-dodec-2-enoate + FMN + H2O + hn
-
-
-
-
?
(E)-oct-2-enal + FMNH2 + O2
(2E)-oct-2-enoate + FMN + H2O + hn
-
-
-
-
?
(E)-tetradec-2-enal + FMNH2 + O2
(E)-tetradec-2-enoate + FMN + H2O + hn
-
-
-
-
?
(E)-tetradec-2-enal + FMNH2 + O2
(E)-tetradec-2-enoate + FMN + H2O + hn
-
-
-
-
?
(E)-tetradec-2-enal + FMNH2 + O2
(E)-tetradec-2-enoate + FMN + H2O + hn
-
-
-
-
?
a long-chain aldehyde + FMNH2 + O2
a long-chain fatty acid + FMN + H2O + hv
-
supply of FNH2 can be achieved by 1-benzyl-1,4-dihydronicotinamide instead of a flavin reductase system
-
-
?
a long-chain aldehyde + FMNH2 + O2
a long-chain fatty acid + FMN + H2O + hv
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
-
a long chain aliphatic aldehyde as substrate
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
-
-
-
-
?
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
348545, 348546, 348547, 348548, 348549, 348550, 348551, 348552, 348553, 348554, 348555, 348557, 348558, 348559, 348560, 348562, 348564, 348565, 348566, 348567, 348568, 348569, 348570, 348571, 348572, 348573, 348574, 348575, 348576, 348577, 348579, 348581, 348582, 348583, 348584, 348585, 348587, 348588, 348589, 348597, 348599, 348600, 348601, 348602, 348604, 348607, 348608
-
-
ir
decanal + FMNH2 + O2
decanoate + FMN + H2O + hn
-
formation of a 4a-hydroperoxy-FMN intermediate II
-
-
ir
decanal + FMNH2 + O2
decanoic acid + FMN + H2O + hv
-
-
light emission at 490 nm
-
?
decanal + FMNH2 + O2
decanoic acid + FMN + H2O + hv
-
-
light emission at 490 nm
-
?
decanal + FMNH2 + O2
decanoic acid + FMN + H2O + hv
-
-
-
?
decanal + FMNH2 + O2
decanoic acid + FMN + H2O + hv
-
-
light emission at 490 nm
-
?
decanal + FMNH2 + O2
decanoic acid + FMN + H2O + hv
-
-
light emission at 490 nm
-
?
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
-
-
348545, 348546, 348547, 348548, 348549, 348550, 348551, 348552, 348553, 348554, 348555, 348557, 348558, 348559, 348560, 348562, 348564, 348565, 348566, 348567, 348568, 348569, 348570, 348571, 348572, 348573, 348574, 348575, 348576, 348577, 348579, 348581, 348582, 348583, 348584, 348585, 348587, 348588, 348589, 348597, 348599, 348600, 348601, 348602, 348604, 348607, 348608
-
-
ir
luciferin + O2 + ATP
oxyluciferin + AMP + diphosphate + CO2 + light
-
-
-
-
ir
luciferin + O2 + ATP
oxyluciferin + AMP + diphosphate + CO2 + light
-
-
-
-
ir
n-decanal + FMNH2 + O2
n-decanoate + FMN + H2O + hn
-
3-step process via H2O2 as intermediate
generation of blue-green light of wavelength 490 nm
-
ir
n-decanal + FMNH2 + O2
n-decanoate + FMN + H2O + hn
-
3-step process via H2O2 as intermediate
generation of blue-green light of wavelength 490 nm
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
-
-
348545, 348546, 348547, 348548, 348549, 348550, 348551, 348552, 348553, 348554, 348555, 348557, 348558, 348559, 348560, 348562, 348564, 348565, 348566, 348567, 348568, 348569, 348570, 348571, 348572, 348573, 348574, 348575, 348576, 348577, 348579, 348581, 348582, 348583, 348584, 348585, 348587, 348588, 348589, 348597, 348599, 348600, 348601, 348602, 348604, 348607, 348608
-
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
-
3-step process via H2O2 as intermediate
generation of blue-green light of wavelength 490 nm
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
-
3-step process via H2O2 as intermediate
generation of blue-green light of wavelength 490 nm
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
-
long-chain aldehydes
long-chain fatty acids, bioluminescence reaction
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
-
formation of a 4a-hydroperoxy-FMN intermediate II
-
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
-
formation of a C4a-hydroperoxyflavin intermediate
-
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hnu
-
reduced FMN, i.e. FMNH2, generated by several species of flavin reductases, is utilized along with a long-chain aliphatic aldehyde and molecular oxygen by luciferase as substrates for the bioluminescence reaction, direct transfer of reduced flavin cofactor and reduced flavin product of reductase to luciferase, NADPH-specific FMN reductase and luciferase form a complex in vivo, reduction of reductase-bound FMN cofactor by NADPH is reversible, allowing the cellular contents of NADP+ and NADPH as a factor for the regulation of the production of FMNH2 by FRPVh for luciferase bioluminescence, overview
-
-
?
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hnu
-
reduced FMN, i.e. FMNH2, generated by several species of flavin reductases, is utilized along with a long-chain aliphatic aldehyde and molecular oxygen by luciferase as substrates for the bioluminescence reaction, direct transfer of reduced flavin cofactor and reduced flavin product of reductase to luciferase, NADPH-specific FMN reductase and luciferase form a complex in vivo, reduction of reductase-bound FMN cofactor by NADPH is reversible, allowing the cellular contents of NADP+ and NADPH as a factor for the regulation of the production of FMNH2 by FRPVh for luciferase bioluminescence, overview
-
-
?
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hv
-
-
the enzyme is emitting blue-green light at 490 nm
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
-
-
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
-
-
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
-
-
-
-
?
additional information
?
-
-
aldehydes of chain-length 8 or more required
-
-
?
additional information
?
-
-
electrochemical luminescence system using bacterial luciferase, in which one of the substrates, FMNH2, is regenerated by the electrochemical reduction of FMN at a Pt-mesh electrode
-
-
?
additional information
?
-
-
enzyme accepts unsaturated aldehydes as substrates but light emission drops drastically compared to saturated aldehydes. The onset and the decay rate of bioluminescence are much slower, when using unsaturated substrates. As a result the duration of the light emission is doubled
-
-
?
additional information
?
-
-
enzyme accepts unsaturated aldehydes as substrates but light emission drops drastically compared to saturated aldehydes. The onset and the decay rate of bioluminescence are much slower, when using unsaturated substrates. As a result the duration of the light emission is doubled
-
-
?
additional information
?
-
-
the Gluc luciferase retains its luminescence output in the stationary phase of growth and exhibits enhanced stability during exposure to low pH, hydrogen peroxide, and high temperature
-
-
?
additional information
?
-
-
LuxG is a NADH:FMN oxidoreductase that supplies FMNH? to luciferase in vivo
-
-
?
additional information
?
-
-
enzyme accepts unsaturated aldehydes as substrates but light emission drops drastically compared to saturated aldehydes. The onset and the decay rate of bioluminescence are much slower, when using unsaturated substrates. As a result the duration of the light emission is doubled
-
-
?
additional information
?
-
-
LuxG is a NADH:FMN oxidoreductase that supplies FMNH? to luciferase in vivo
-
-
?
additional information
?
-
-
aldehydes of chain-length 8 or more required
-
-
?
additional information
?
-
-
the decay rate of the enzyme is determined by residue Glu175 of the central region of the LuxA subunit, distinction between slow and fast decay luciferases is primarily due to differences in aldehyde affinity and in the decomposition of the luciferase-flavin-oxygen intermediate
-
-
?
additional information
?
-
-
substrate specificity and quantum yield of mutant E175G as a function of aldehyde chain length
-
-
?
additional information
?
-
-
LuxG is a NADH:FMN oxidoreductase that supplies FMNH- to luciferase in vivo
-
-
?
additional information
?
-
-
aldehydes of chain-length 8 or more required
-
-
?
additional information
?
-
-
complex formation in a 1:1 molar ratio between monomeric, but not dimeric, NADPH:FMN oxidoreductase FRP and luciferase for direct transfer of cofactor FMNH2
-
-
?
additional information
?
-
-
the enzyme plays a role in protection of cells against oxidative stress
-
-
?
additional information
?
-
-
substrate specificities of mutant enzymes and wild-type enzyme, overview
-
-
?
additional information
?
-
-
Vibrio harveyi NADPH-specific flavin reductase FRP transfers reduced riboflavin-5'-phosphate to luciferase by both free diffusion and direct transfer, resulting inbioluminescence production, FRP:luciferase coupled bioluminescence reaction, overview, increases in oxygen concentration lead to gradual decreases of the peak bioluminescence intensity, Km for FMN, and Km for NADPH of NADPH-specific flavin reductase in the coupled reaction with luciferase
-
-
?
additional information
?
-
-
active site hydrophobicity is critical to the bioluminescence activity of Vibrio harveyi luciferase
-
-
?
additional information
?
-
-
the 4a-hydroperoxy-4a,5-dihydroFMN intermediate luciferase transforms from a low quantum yield IIx to a high quantum yield IIy fluorescent species on exposure to excitation light
-
-
?
additional information
?
-
-
FMNH2 binds to a mobile loop of 29 amino acids in the luciferase protein, loop modeling of ligand-free and -bound enzyme, conformation and dynamics, overview
-
-
?
additional information
?
-
-
enzyme accepts unsaturated aldehydes as substrates but light emission drops drastically compared to saturated aldehydes. The onset and the decay rate of bioluminescence are much slower, when using unsaturated substrates. As a result the duration of the light emission is doubled
-
-
?
additional information
?
-
-
enzyme accepts unsaturated aldehydes as substrates but light emission drops drastically compared to saturated aldehydes. The onset and the decay rate of bioluminescence are much slower, when using unsaturated substrates. As a result the duration of the light emission is doubled
-
-
?
