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(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)-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
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
-
-
-
-
?
a long-chain aldehyde + FMNH2 + O2
a long-chain fatty acid + FMN + H2O + hv
aldehyde + FMNH2 + O2
?
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
beetle luciferin + FMNH2 + O2
?
-
-
-
-
ir
coelenterazine + FMNH2 + O2
CO2 + coelenteramide + FMN + light + H2O
-
an imidazolopyrazine derivative
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
decanal + FMNH- + O2
decanoic acid + FMN + H2O + hv
decanal + FMNH2 + O2
decanoate + FMN + H2O + hn
decanal + FMNH2 + O2
decanoate + FMN + H2O + hnu
-
-
-
-
?
decanal + FMNH2 + O2
decanoate + FMN + H2O + hv
-
-
-
-
ir
decanal + FMNH2 + O2
decanoic acid + FMN + H2O + hnu
-
-
-
-
?
decanal + FMNH2 + O2
decanoic acid + FMN + H2O + hv
decanal + riboflavin + O2
?
-
riboflavin is a very poor substrate for bacterial luciferase
-
-
?
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
dodecanal + FMNH2 + O2
dodecanoate + FMN + H2O + hn
dodecanal + FMNH2 + O2
dodecanoic acid + FMN + H2O + hv
-
-
-
-
?
dodecyl aldehyde + FMNH + O2
?
-
-
-
-
?
fatty aldehyde + FMNH2 + O2
fatty acid + FMN + H2O + hn
-
-
-
-
ir
hexachlorethane + e-
tetrachlorethylene + Cl-
-
-
-
-
?
luciferin + O2 + ATP
oxyluciferin + AMP + diphosphate + CO2 + light
myristic aldehyde + FMNH + O2
myristic acid + FMN + H2O + light
-
-
-
-
?
n-caprinaldehyde + FMNH2 + O2
n-caprinoate + FMN + H2O + hv
-
-
-
-
ir
n-decanal + FMNH2 + O2
n-decanoate + FMN + H2O + hn
nonanal + FMNH2 + O2
nonanoate + FMN + H2O + hn
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
octanal + FMNH2 + O2
octanoate + FMN + H2O + hn
-
-
-
-
ir
pentachlorethane + e-
trichlorethylene + Cl-
-
-
-
-
?
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hnu
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hv
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
undecanal + FMNH2 + O2
undecanoate + FMN + H2O + hn
-
-
-
-
ir
additional information
?
-
(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)-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)-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)-oct-2-enal + FMNH2 + O2
(2E)-oct-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
-
-
-
-
?
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
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
-
?
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 + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
?
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
-
ir
decanal + FMNH- + O2
decanoic acid + FMN + H2O + hv
-
-
-
-
?
decanal + FMNH- + O2
decanoic acid + FMN + H2O + hv
-
-
-
-
?
decanal + FMNH- + O2
decanoic acid + FMN + H2O + hv
-
-
-
-
?
decanal + FMNH2 + O2
decanoate + FMN + H2O + hn
-
-
-
-
?
decanal + FMNH2 + O2
decanoate + FMN + H2O + hn
-
-
-
-
?
decanal + FMNH2 + O2
decanoate + FMN + H2O + hn
-
-
-
-
?
decanal + FMNH2 + O2
decanoate + FMN + H2O + hn
-
-
-
-
?
decanal + FMNH2 + O2
decanoate + FMN + H2O + hn
-
-
-
-
ir
decanal + FMNH2 + O2
decanoate + FMN + H2O + hn
-
formation of a 4a-hydroperoxy-FMN intermediate II
-
-
ir
decanal + FMNH2 + O2
decanoate + FMN + H2O + hn
-
-
-
-
?
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
-
?
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
-
-
-
-
?
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
-
-
-
-
ir
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
-
-
-
-
?
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
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
-
-
-
?
dodecanal + FMNH + O2
dodecanoic acid + FMN + H2O + light
-
-
-
-
ir
dodecanal + FMNH2 + O2
dodecanoate + FMN + H2O + hn
-
-
-
-
?
dodecanal + FMNH2 + O2
dodecanoate + FMN + H2O + hn
-
-
-
-
?
dodecanal + FMNH2 + O2
dodecanoate + FMN + H2O + hn
-
-
-
-
?
dodecanal + FMNH2 + O2
dodecanoate + FMN + H2O + hn
-
-
-
-
?
dodecanal + FMNH2 + O2
dodecanoate + FMN + H2O + hn
-
-
-
-
ir
dodecanal + FMNH2 + O2
dodecanoate + FMN + H2O + hn
-
-
-
-
?
FMNH + O2
FMN + H2O2
-
-
-
-
?
FMNH + O2
FMN + H2O2
-
-
-
-
?
FMNH + O2
FMN + H2O2
-
-
-
-
?
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
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
-
-
-
-
ir
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
-
-
-
-
?
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
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
-
-
-
?
octanal + FMNH + O2
octanoic acid + FMN + H2O + light
-
-
-
-
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
-
-
-
-
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hv
-
-
the enzyme is emitting blue-green light at 490 nm
-
?
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hv
-
-
-
-
?
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hv
-
-
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
-
-
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
-
-
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
-
-
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
-
-
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
-
-
-
-
ir
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
?
-
-
luminescence pathway, overview
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
beetle luciferin + FMNH2 + O2
?
-
-
-
-
ir
coelenterazine + FMNH2 + O2
CO2 + coelenteramide + FMN + light + H2O
-
an imidazolopyrazine derivative
-
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
fatty aldehyde + FMNH2 + O2
fatty acid + FMN + H2O + hn
-
-
-
-
ir
luciferin + O2 + ATP
oxyluciferin + AMP + diphosphate + CO2 + light
n-caprinaldehyde + FMNH2 + O2
n-caprinoate + FMN + H2O + hv
-
-
-
-
ir
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hn
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hnu
RCHO + FMNH2 + O2
RCOOH + FMN + H2O + hv
-
-
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
-
-
-
-
ir
additional information
?
-
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
-
-
-
-
?
an aldehyde + FMNH2 + O2
a carboxylate + FMN + H2O + hnu
-
-
-
-
?
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
-
-
-
-
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 -
-
ir
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
-
-
-
-
ir
luciferin + O2 + ATP
oxyluciferin + AMP + diphosphate + CO2 + light
-
-
-
-
ir
luciferin + O2 + ATP
oxyluciferin + AMP + diphosphate + CO2 + light
-
-
-
-
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
-
-
-
-
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
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
luminescence pathway, overview
-
-
?
additional information
?
-
-
the enzyme plays a role in protection of cells against oxidative stress
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2,2-diphenylpropylamine
-
-
2,3-Dichloro-(6-phenylphenoxy)ethylamine
2,4-dinitrofluorobenzene
-
i.e. Sanger's reagent
2-Bromodecanal
-
protection by dithiothreitol or mercaptoethanol
2-diethylaminoethyl-2,2-diphenylvalerate
2-methyl-1,4-benzoquinone
-
-
2-methyl-5-isopropyl-1,4-benzoquinone
-
-
5-decyl-4a-hydroxy-4a,5-dihydroriboflavin-5'-phosphate
-
binding and fluorescence quantum yield studies of the substance as a model, complexed with the enzyme in a 1:1 molcular ratio leading to 80% and 90% inhibition of wild-type and mutant C106A at 0.01 mM, respectively, binds to the active site
6-(3'-(R)-myristyl) flavin adenine mononucleotide
binds noncovalently to the enzyme dimer. Addition of recombinant apo-LuxF captures myrFMN and thereby relieves the inhibitory effect
8-Anilino-1-naphthalenesulfonate
dodecanamide
-
inhibits bacterial luciferase luminescence reaction. By injecting the dodecaneamide into the bacterial luciferase system, the luminescence intensity decreases to about half of the initial intensity
fullerenol
-
fullerenols suppress bioluminescent intensity at concentrations above 0.01 g/l and above 0.001 g/l for C60O2-4(OH)20-24 and Fe0.5C60(OH)xOy, respectively
methanol
-
bacterial luciferase luminescence intensity decreases to the steady state depending on the methanol concentration
N,N-Diethyl-2,4-dichloro-(6-phenylphenoxy)ethylamine
-
-
N-ethylmaleimide
-
protection by substrates
N-phenacylthiazolium bromide
-
highly selective inhibition
pifithrin-alpha
-
highly selective inhibitor in vivo and in vitro
potassium iodide
-
quenches the fluorescence of FMN effectively at 0.2 M, and enhances the decay of wild-type and HFOOH enzymes, the wild-type enzyme forms an inactive complex with KI
Proteases
-
trypsin, chymotrypsin
-
Urea
-
denaturation curve, thermodynamics, wild-type and mutants, overview
1-Dodecanol
-
-
2,3-Dichloro-(6-phenylphenoxy)ethylamine
-
-
2,3-Dichloro-(6-phenylphenoxy)ethylamine
-
-
2,3-Dichloro-(6-phenylphenoxy)ethylamine
-
-
2-diethylaminoethyl-2,2-diphenylvalerate
-
-
2-diethylaminoethyl-2,2-diphenylvalerate
-
-
2-diethylaminoethyl-2,2-diphenylvalerate
-
-
8-Anilino-1-naphthalenesulfonate
-
-
8-Anilino-1-naphthalenesulfonate
-
-
8-Anilino-1-naphthalenesulfonate
-
-
8-Anilino-1-naphthalenesulfonate
-
inhibitor binding site separate from FMN-binding site by 30 A
8-Anilino-1-naphthalenesulfonate
-
-
amino group reagents
-
-
-
amino group reagents
-
-
-
amino group reagents
-
-
-
ethoxyformic anhydride
-
-
ethoxyformic anhydride
-
-
ethoxyformic anhydride
-
-
imidazole reagents
-
-
-
n-decanal
-
reversible substrate inhibition, depending on phosphate concentration
sulfhydryl reagents
-
-
additional information
-
1-hexanol does not inhibit the enzyme luminescence
-
additional information
-
hydrophobicity of the quinone plays a role in the non-specific inhibition mechanism of xenobiotic molecules in the bacterial bioluminescence system via altering the rotational mobility of the endogenous flavin in the luciferase. Added quinone reduces the averaged binding affinity of the endogenous FMN to the active site of luciferase by increasing the fraction of the weak FMN binding sites of luciferase
-
additional information
-
luxA mutant and luxB mutant strains are more sensitive to oxidants like H2O2, cumene hydroperoxide, tert-butyl hydroperoxide, or ferrous sulfate, than the wild-type strain, growth behaviour overview
-
additional information
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.26
4-N,N-(dimethyl)aminonaphthalene-9-N-(11-aldehydedodecyl)-1,8-dicarboximide
-
pH 7.0, temperature not specified in the publication
0.72
4-N,N-(dimethyl)aminonaphthalene-9-N-(9-aldehyde-decyl)-1,8-dicarboximide
-
pH 7.0, temperature not specified in the publication
0.72
4-N-(11-aldehyde-dodecyl)-7-N,N-dimethylsulfonic-2,1,3-benzoxadiazole
-
pH 7.0, temperature not specified in the publication
1.79
4-N-(9-aldehyde-decyl)-7-N,N-dimethylsulfonic-2,1,3-benzoxadiazole
-
pH 7.0, temperature not specified in the publication
0.001 - 0.01
aldehydes
-
-
0.0009
FMN
-
in the presence of different flavin concentrations, 0.001 mM Fre oxidoreductase, 10 mM decanal, and 0.01 mM NADPH and 0.005 mM luciferase
0.0012 - 0.009
n-decanal
-
depending on buffer system
0.0013
riboflavin
-
in the presence of different flavin concentrations, 0.001 mM Fre oxidoreductase, 10 mM decanal, and 0.01 mM NADPH and 0.005 mM luciferase
additional information
additional information
-
0.0003
decanal
-
wild type, 50 mM phosphate
0.0004
decanal
-
recombinant mutant alphaF261S, pH 7.0, 25°C
0.0004
decanal
-
recombinant mutant alphaG275I, pH 7.0, 25°C
0.001
decanal
-
recombinant wild-type enzyme, pH 7.0, 25°C
0.00101
decanal
-
pH 7.0, 23°C, recombinant mutant F49Y
0.00113
decanal
-
recombinant wild type enzyme, at 22°C, pH not specified in the publication
0.0013
decanal
-
pH 7.0, 23°C, recombinant mutant F46A
0.0016
decanal
-
recombinant mutant alphaF261Y, pH 7.0, 25°C
0.0016
decanal
-
pH 7.0, 23°C, recombinant wild-type enzyme
0.0016
decanal
-
pH 7.0, 23°C, recombinant wild-type enzyme and mutant A74G
0.00165
decanal
-
luciferase-mOrange fusion enzyme, at 22°C, pH not specified in the publication
0.0017
decanal
-
recombinant mutant alphaF261A, pH 7.0, 25°C
0.0018
decanal
-
recombinant mutant alphaG275P, pH 7.0, 25°C
0.0021
decanal
-
alphaR107S, 50 mM phosphate
0.0022
decanal
-
alphaR107E, 50 mM phosphate
0.0022
decanal
-
recombinant mutant alphaG275A, pH 7.0, 25°C
0.0023
decanal
-
pH 7.0, 23°C, recombinant mutant E328Q
0.0024
decanal
-
pH 7.0, 23°C, recombinant mutant F117S
0.0024
decanal
-
pH 7.0, 23°C, recombinant mutant F46Y
0.0026
decanal
-
pH 7.0, 23°C, recombinant mutant F46S
0.0027
decanal
-
recombinant mutant alphaG275F, pH 7.0, 25°C
0.0027
decanal
-
pH 7.0, 23°C, recombinant mutant F114Y
0.003
decanal
-
pH 7.0, 23°C, recombinant mutants F49D, F117A, and F49A
0.0031
decanal
-
alphaR107A, 50 mM phosphate
0.0031
decanal
-
pH 7.0, 23°C, recombinant mutant F117D
0.0032
decanal
-
pH 7.0, 23°C, recombinant mutant F46D
0.0033
decanal
-
pH 7.0, 23°C, recombinant mutant E328A
0.0033
decanal
-
pH 7.0, 23°C, recombinant mutant F49S
0.0037
decanal
-
recombinant mutant alphaG284P, pH 7.0, 25°C
0.0045
decanal
-
pH 7.0, 23°C, recombinant mutant E328F
0.0046
decanal
-
recombinant mutant alphaF261D, pH 7.0, 25°C
0.005
decanal
-
pH 7.0, 23°C, recombinant mutant E328D
0.0051
decanal
-
pH 7.0, 23°C, recombinant mutant F117Y
0.0073
decanal
-
pH 7.0, 23°C, recombinant mutant F114D
0.008
decanal
-
wild-type
0.0083
decanal
-
pH 7.0, 23°C, recombinant mutant F114S
0.0093
decanal
-
pH 7.0, 23°C, recombinant mutant F114A
0.0095
decanal
-
pH 7.0, 23°C, recombinant mutant E328H
0.0097
decanal
-
pH 7.0, 23°C, recombinant mutant E328L
0.01
decanal
-
mutant K286A
0.0105
decanal
-
mutant K283A
0.0173
decanal
-
pH 7.0, 23°C, recombinant mutant A74F
0.11
decanal
-
pH 7.0, temperature not specified in the publication
0.00015
FMNH
-
alpha subunit
0.00058
FMNH
-
beta subunit
0.0008
FMNH
-
wild type, 10 mM phosphate
0.0018
FMNH
-
wild type, 300 mM phosphate
0.0038
FMNH
-
alphaR107S, 10 mM phosphate
0.0049
FMNH
-
alphaR107S, 300 mM phosphate
0.0081
FMNH
-
alphaR107A, 10 mM phosphate
0.0095
FMNH
-
alphaR107A, 300 mM phosphate
0.0114
FMNH
-
alphaR107E, 300 mM phosphate
0.0234
FMNH
-
alphaR107E, 10 mM phosphate
0.00018
FMNH2
-
luciferase-mOrange fusion enzyme, at 22°C, pH not specified in the publication
0.0002
FMNH2
-
pH 7.0, 23°C, recombinant mutant F114S
0.0002
FMNH2
-
pH 7.0, 23°C, recombinant mutants E328Q and E328H
0.0002
FMNH2
-
recombinant wild type enzyme, at 22°C, pH not specified in the publication
0.0003
FMNH2
-
recombinant wild-type enzyme, pH 7.0, 25°C
0.0003
FMNH2
-
pH 7.0, 23°C, recombinant mutants E328L and E328A
0.0003
FMNH2
-
pH 7.0, 23°C, recombinant mutants F46Y, F114A, F117Y, and F114Y
0.0004
FMNH2
-
pH 7.0, 23°C, recombinant mutant E328D
0.0006
FMNH2
-
recombinant mutant alphaG284P, pH 7.0, 25°C
0.0006
FMNH2
-
pH 7.0, 23°C, recombinant mutant F49Y
0.0006
FMNH2
-
pH 7.0, 23°C, recombinant wild-type enzyme
0.0007
FMNH2
-
pH 7.0, 23°C, recombinant mutant F49S
0.001
FMNH2
-
pH 7.0, 23°C, recombinant mutant F114D
0.0013
FMNH2
-
pH 7.0, 23°C, recombinant mutant F117S
0.0013
FMNH2
-
pH 7.0, 23°C, recombinant mutant F49D
0.0015
FMNH2
-
pH 7.0, 23°C, recombinant mutant A74G
0.0015
FMNH2
-
pH 7.0, 23°C, recombinant mutant F117A
0.0022
FMNH2
-
recombinant mutant alphaG275P, pH 7.0, 25°C
0.0027
FMNH2
-
pH 7.0, 23°C, recombinant mutant F49A
0.0039
FMNH2
-
pH 7.0, 23°C, recombinant mutant E328F
0.0043
FMNH2
-
pH 7.0, 23°C, recombinant mutant F46S
0.0075
FMNH2
-
recombinant mutant alphaF261D, pH 7.0, 25°C
0.0087
FMNH2
-
pH 7.0, 23°C, recombinant mutant A74F
0.0123
FMNH2
-
pH 7.0, 23°C, recombinant mutant F46A
0.0148
FMNH2
-
pH 7.0, 23°C, recombinant mutant F46D
0.0192
FMNH2
-
recombinant mutant alphaF261Y, pH 7.0, 25°C
0.0281
FMNH2
-
recombinant mutant alphaF261A, pH 7.0, 25°C
0.0358
FMNH2
-
recombinant mutant alphaG275A, pH 7.0, 25°C
0.0369
FMNH2
-
recombinant mutant alphaF261S, pH 7.0, 25°C
0.0411
FMNH2
-
recombinant mutant alphaG275F, pH 7.0, 25°C
0.052
FMNH2
-
pH 7.0, 23°C, recombinant mutant F117D
0.0584
FMNH2
-
recombinant mutant alphaG275I, pH 7.0, 25°C
additional information
additional information
-
affinity and dissociation constants for FMNH2 of wild-type and mutants enzymes, kinetics
-
additional information
additional information
-
detailed reaction and folding kinetics, thermodynamics
-
additional information
additional information
-
enzyme activities in complex formation, kinetics, dissociation constants
-
additional information
additional information
-
kinetics, substrate and cofactor binding
-
additional information
additional information
-
stopped flow spectroscopy
-
additional information
additional information
-
kinetics of the FRP:luciferase coupled bioluminescence reaction
-
additional information
additional information
-
stopped-flow and Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
stopped-flow kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of FMN reductase-luciferase complex formation, overview
-
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D232G
-
random mutagenesis, 63% of wild-type luminescence activity
E175G
-
random mutagenesis, the single point mutation leads to increased decay rate of the enzyme, 0.9% of wild-type luminescence activity
E175G/N199D
-
random mutagenesis, 0.1% of wild-type luminescence activity
K202R
-
random mutagenesis, 95% of wild-type luminescence activity
M190T
-
random mutagenesis, 29% of wild-type luminescence activity
T198S
-
random mutagenesis, 84% of wild-type luminescence activity
A74F
-
site-directed mutagenesis, the mutant shows reduced activity and increased Km compared to the wild-type enzyme
A74G
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
A75G
-
site-directed mutagenesis, activity similar to the wild-type enzyme
A75G/C106V/V173A
-
site-directed mutagenesis, alpha-subunit residues, reduced activity compared to the wild-type enzyme, further red shift of emission spectrum
A75G/C106V/V173C
-
site-directed mutagenesis, alpha-subunit residues, reduced activity compared to the wild-type enzyme, further red shift of emission spectrum
A75G/C106V/V173S
-
site-directed mutagenesis, alpha-subunit residues, reduced activity compared to the wild-type enzyme, further red shift of emission spectrum
A75G/C106V/V173T
-
site-directed mutagenesis, alpha-subunit residues, reduced activity compared to the wild-type enzyme, further red shift of emission spectrum
A81H
-
site-directed mutagenesis, residue of the alpha-subunit, mutant shows 13% of wild-type activity
alphaDELTA262-290beta
-
four times higher affinity for FMN than wild type
alphaF114A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF114D
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF114S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF114Y
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
alphaF117A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF117D
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF117S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF117Y
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
alphaF327A
-
site-directed mutagenesis, mutant activity is similar to the wild-type enzyme
alphaF46A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF46D
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF46S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF46Y
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
alphaF49A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF49D
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF49S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme due to reduced hydrophobicity of the active site
alphaF49Y
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
alphaF6A
-
site-directed mutagenesis, mutant activity is similar to the wild-type enzyme
alphaR107A
-
lower affinity for FMNH
alphaR107E
-
lower affinity for FMNH
alphaR107S
-
lower affinity for FMNH
C106A
-
site-directed mutagenesis, catalytic properties are similar to the wild-type enzyme, mutant shows 60% of wild-type quantum yield
C106V
-
site-directed mutagenesis, highly reduced ability to stabilize the reaction intermediate due to interaction between Val106 and Ala75 side chains, and therefore highly reduced activity and increased thermal lability compared to the wild-type enzyme
C106V/A75G
-
site-directed mutagenesis, mutation of Ala75 restores about 90% of the activity abolished by mutation of Cys106, shift in the light emission spectrum to that of Photobacterium phosphoreum possessing Val and Gly at positions 106 and 75, respectively
D262A
-
90% reduced activity with octanal, 36% reduced activity with decanal, activity with dodecanal as the wild-type
D265A
-
activity with octanal as the wild-type, 81% reduced activity with decanal, complete loss of dodecanal activity
D271A
-
complete loss of octanal and decanal activity, 18% reduced activity with dodecanal
E328A
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme, the activity is rescued by addition of sodium acetate, but not by phosphate, at pH 6.0-8.0 with increasing activity at lower pH
E328D
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme
E328F
-
site-directed mutagenesis, the mutant shows reduced activity and increased Km compared to the wild-type enzyme
E328H
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme
E328L
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme
E328Q
-
site-directed mutagenesis, the mutant shows highly reduced activity and increased Km compared to the wild-type enzyme
F261A
-
site-directed mutagenesis, residue of the alpha-subunit, 0.19% of the wild-type activity, the bulky and hydrophobic nature of the alphaF261 residue is critical for activity
F261D
-
site-directed mutagenesis, residue of the alpha-subunit, 0.004% of the wild-type activity, the bulky and hydrophobic nature of the alphaF261 residue is critical for activity
F261S
-
site-directed mutagenesis, residue of the alpha-subunit, 0.13% of the wild-type activity, the bulky and hydrophobic nature of the alphaF261 residue is critical for activity
F261Y
-
site-directed mutagenesis, residue of the alpha-subunit, 2-3% of the wild-type activity, the bulky and hydrophobic nature of the alphaF261 residue is critical for activity
G275A
-
site-directed mutagenesis, residue of the alpha-subunit, 27% of the wild-type activity, the torsional flexibility of the alphaG275 residue is critical for activity
G275F
-
site-directed mutagenesis, residue of the alpha-subunit, 6-7% of the wild-type activity, the torsional flexibility of the alphaG275 residue is critical for activity
G275I
-
site-directed mutagenesis, residue of the alpha-subunit, 15% of the wild-type activity, the torsional flexibility of the alphaG275 residue is critical for activity
G275P
-
site-directed mutagenesis, residue of the alpha-subunit, 0.04% of the wild-type activity, the torsional flexibility of the alphaG275 residue is critical for activity
G284P
-
site-directed mutagenesis, residue of the alpha-subunit, 1-2% of the wild-type activity
H285A
-
26% reduced activity with octanal, 74% reduced activity with decanal, complete loss of dodecanal activity
H44A
1.5% of wild-type activity
H44D
2.1% of wild-type activity
H44N
2.2% of wild-type activity
H45A
1.7% of wild-type activity
H4A/H45A
1.95% of wild-type activity
H81A
-
site-directed mutagenesis, residue of the beta-subunit, mutant shows 59% of wild-type activity
H81A/E89D
-
site-directed mutagenesis, residues of the beta-subunit, mutant shows 13% of wild-type activity
H82A
-
site-directed mutagenesis, residue of the beta-subunit, mutant shows 22% of wild-type activity
K274A
-
89% reduced activity with octanal, 21% reduced activity with decanal, 81% reduced activity with dodecanal
K283A
-
complete loss of octanal and decanal activity, 96% reduced activity with dodecanal, does not significantly impede binding of decanal, results in destabilization of intermediate II, results in a loss in quantum yield comparable with that of the loop deletion mutant, binds reduced flavin more weakly
K286A
-
92% reduced activity with octanal, complete loss of decanal activity, 87% reduced activity with dodecanal, does not significantly impede binding of decanal, increase in exposure of reaction intermediates to a dynamic quencher, results in a loss in quantum yield comparable with that of the loop deletion mutant, binds reduced flavin more weakly
R291A
-
77% reduced activity with octanal, 58% reduced activity with decanal, 71% reduced activity with dodecanal
V173A
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173C
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173F
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173H
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173I
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173L
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173N
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173S
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
V173T
-
site-directed mutagenesis, alpha-subunit residue, reduced activity and decreased stability of the C4a-hydroperoxyflavin intermediate compared to the wild-type enzyme, red shift of emission spectrum
W277A
-
11% reduced activity with octanal, 50% reduced activity with decanal and dodecanal
Y151A
binds FMNH2 more weakly in comparison to the wild-type, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
Y151D
binds FMNH2 more weakly in comparison to the wild-type, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
Y151K
binds FMNH2 more weakly in comparison to the wild-type, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
Y151R
binds FMNH2 more weakly in comparison to the wild-type, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
Y151T
binds FMNH2 more weakly in comparison to the wild-type, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
Y151W
least active mutant, binds reduced flavin with wild-type affinity, substitution at position 151 on the beta subunit causes reductions in activity and total quantum yield
alphaH44A
-
decreased bioluminescence
alphaH44A
-
rapid decay of the 4a-hydroperoxy-4a,5-dihydroFMN intermediate enzyme, HFOOH, in the mutant
additional information
-
improvement of a tagging system, allowing real-time monitoring in vivo and in vitro, for luciferase by construction of a highly active, constitutive promoter resulting in a 100fold higher recombinant activity compared to native activity
additional information
-
Saccharomyces cerevisiae recombinantly expressing the Vibrio harveyi luciferase produces bright and stable luminescence, transformed yeast strains can grow on 0.5% v/v Z-9-tetradecenal, but die on 0.005% v/v decanal
additional information
-
substrate specificities of mutant enzymes and wild-type enzyme, overview, changes in the kinetics and emission spectrum on mutation of the chromophore-binding platform
additional information
-
immobilization of the FMN reductase-luciferase complex
additional information
-
codon optimization of the luxCDE and frp genes, e.g. adaptation of the bacterial protein to mammalian temperature of 37°C, detailed overview
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amplified from the pJHD500 plasmid and ligated into a pET21b vector, expressed from pZCH2 in an Escherichia coli BL21 (lambdaDE3) cell line after growth to an OD600 of 0.5
coexpression of luciferase and cytochrome P-450
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expressed in Escherichia coli BL21(DE3) and HEK-293T cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli from pJHD500, ligated into a pET21b vector. Luciferase subcloned from pZCH2 into a pASKIBA-3c vector with the restriction sites XbaI and XhoI. The resulting luciferase containing a strep-II tag on the C terminus of the beta-subunit (pZCB4) expressed
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expressed in Escherichia coli JM109 (native enzyme) and BL21(DE3) cells (luciferase-mOrange fusion enzyme)
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expressed in NIH-3T3 cells
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expressed in Pseudomonas putida mt-2
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expression analysis, cloning into expression vector pPL2lux useable as a reporter system based on the luciferase activity of the enzyme, overview
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expression in Bacillus subtilis and in Escherichia coli
expression in different Escherichia coli strains, which are wild-type, or deficient in gene clpA, clpB, and clpX encoding Hsp chaperones, respectively
expression in Escherichia coli
expression in Escherichia coli strain JM101
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expression in Pseudomonas putida
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expression of fused luxA and luxB genes and also luxF gene in Escherichia coli and Nicotiana plumbaginifolia
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expression of fused luxA and luxB genes in Escherichia coli
expression of fused luxA and luxB genes in Saccharomyces cerevisiae, Bacillus subtilis, plant cells, plasmid expression vector and in Escherichia coli
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expression of luxA gene in Escherichia coli
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expression of seperated luxA and luxB gene in Escherichia coli JM109
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expression of the enzyme in Mycobacterium tuberculosis under control of the inducible/repressible promotor of the alanine dehydrogenase from Mycobacterium tuberculosis strain H37Rv, usage of a mycobacterial-Escherichia coli shuttle vector
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expression of wild-type and mutant C106A enzymes in Escherichia coli strain JM101
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expression of wild-type and mutant enzymes in Escherichia coli
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expression of wild-type and randomly generated mutants in Escherichia coli strain BL21
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gene Gluc, expression in Mycobacterium smegmatis using an hsp60 promoter, subcloning in Escherichia coli strain DH5alpha
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gene lux, improvement of a tagging system for luciferase by construction of a highly active, constitutive promoter resulting in a 100fold higher recombinant activity compared to native activity
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gene luxA, expression of wild-type and mutant enzymes in Escherichia coli strain JM109
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gene luxAB, expression of wild-type and mutant enzymes in Escherichia coli strain BL21
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gene luxAB, functional coexpression in Saccharomyces cerevisiae with NADPH-specific FMN reductase FRP from Vibrio harveyi, subcloning in Escherichia coli
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genes luxA and luxB, expression under the control of a consensus-type promoter, lacUV5, in Escherichia coli, activity declines abruptly upon entry into the stationary growth phase, while the levels of luciferase proteins remian constant, the phenomenon, termed ADLA, i.e. abrupt decline of luciferase activity, is caused by a decrease in the availability of flavin mononucleotide
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ligated into pET21-b vector, expressed from pZCH2 in Escherichia coli BL21 (lambdaDE3) cell line
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luxCDABE operon, genetic organization, overview
overexpression in Escherichia coli
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overexpression of mutant in XL1 blue MRF' cell line
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overexpression of wild-type and mutant enzymes in Escherichia coli strain JM101
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stable expression, using a bicistronic expression vector, of wild type luxA and luxB, WTA/WTB, codon-optimized luxA and wild type luxB, COA/WTB, and codon-optimized versions of both luxA and luxB genes, COA/COB, in HEK-293 cells, expression analysis, method evaluation and optimization, highest bioluminescence by expression of both codon-optimized genes, overview
the bacterial luciferase lux gene cassette consists of five genes, luxCDABE. The lux operon is re-synthesized through a process of multibicistronic, codon-optimization to demonstrate self-directed bioluminescence emission in a mammalian HEK-293 cell line in vitro and in vivo, overview. To overcome the limitations by FMNH2 supply, co-expression of a constitutively expressed flavin reductase gene frp from Vibrio harveyi is performed leading to a 151fold increased increase in bioluminescence in cells expressing mammalian codon-optimized luxCDE and frp genes
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-
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expression in Bacillus subtilis and in Escherichia coli
expression in Bacillus subtilis and in Escherichia coli
expression in different Escherichia coli strains, which are wild-type, or deficient in gene clpA, clpB, and clpX encoding Hsp chaperones, respectively
-
expression in different Escherichia coli strains, which are wild-type, or deficient in gene clpA, clpB, and clpX encoding Hsp chaperones, respectively
-
expression in Escherichia coli
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expression in Escherichia coli
-
expression of fused luxA and luxB genes in Escherichia coli
-
expression of fused luxA and luxB genes in Escherichia coli
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luxCDABE operon, genetic organization, overview
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luxCDABE operon, genetic organization, overview
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luxCDABE operon, genetic organization, overview
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luxCDABE operon, genetic organization, overview
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luxCDABE operon, genetic organization, overview
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diagnostics
expression of the bacterial luciferase system in mammalian cells for generation of bioreporters for in vivo monitoring and diagnostics technology, method evaluation and optimization, overview
agriculture
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engineering of broad-host-range Erwinia amylovora virus Y2 to enhance its killing activity and for use as a luciferase reporter phage. The reporter phage Y2::luxAB transduces bacterial luciferase into host cells and induces synthesis of large amounts of a LuxAB luciferase fusion. After the addition of aldehyde substrate, bioluminescence can be monitored, and enables rapid and specific detection of low numbers of viable bacteria
agriculture
KJ957766
optimization of fused luxAB expression, quantum yield and application as a reporter gene in plant protoplasts. Luciferase activity is dramatically increased upon use of the optimized gene and the 35S promoter compared to the original luxAB in Arabidopsis and maize cells
analysis
-
enzyme can be used to monitor changes in gene expression as a reporter system in slow-growing mycobacteria, i.e. Mycobacterium tuberculosis strain H37Ra, determination of recombinant enzyme decay rate
analysis
expression of the bacterial luciferase system in mammalian cells for generation of bioreporters for in vivo monitoring and diagnostics technology, method evaluation and optimization, overview
analysis
-
high-throughput, homogeneous, bioluminescent assay for Pseudomonas aeruginosa gyrase inhibitors and other DNA-damaging agents based on a Photorhabdus luminescens luciferase operon transcriptional fusion to a promoter that responds to DNA damage caused by reduced gyrase levels and fluoroquinoline inhibition
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
analysis
-
bioluminescent assay based on a system of coupled enzymatic reactions catalyzed by bacterial luciferase and NADH:FMN-oxidoreductase to monitor toxicity and antioxidant activity of bioactive compounds such as fullerenols, perspective pharmaceutical agents, nanosized particles, water-soluble polyhydroxylated fullerene-60 derivatives. Fullerenols suppress bioluminescent intensity at concentrations above 0.01 g/l and above 0.001 g/l for C60O2-4(OH)20-24 and Fe0.5C60(OH)xOy, respectively
analysis
-
sensitive and selective bacterial luminescence method for the detection of pyruvic acid based on lactate dehydrogenase and the bacterial luciferase-FMN:NADH oxidoreductase bioluminescence in vitro. NADH involved in the LDH reaction system can be quantitatively analyzed by the bioluminescence system. A good linear relationship between the luminescence intensity and pyruvic acid concentration is observed within the range of 0.000140.001 mol/l, and the pyruvic acid detection limit is 0.000085 mol/l
analysis
-
a minimized cascade for Lux with greater ease of use, utilizes a chemoenzymatic reaction with biomimetic nicotinamide 1-benzyl-1,4-dihydronicotinamide in place of the flavin reductase reaction in the Lux system. The minimized cascade reaction can be applied to monitor bioluminescenceof the Lux reporter in eukaryotic cells effectively, and can achieve higher efficiencies than the system with flavin reductase
analysis
fusion of circularly permuted Venus, a bright variant of yellow fluorescent protein, to the C-terminus of subunit LuxB to induce bioluminescence resonance energy transfer (BRET). By using decanal as added substrate, color change and ten-times enhancement of brightness is achieved in Escherichia coli upon expression. Expression of the Venus-fused luciferase in human embryonic kidney cell lines or in Nicotiana benthamiana leaves together with the substrate biosynthesis-related genes (luxC, luxD and luxE) enhances the autonomous bioluminescence
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
analysis
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
biotechnology
-
establishment and evaluation of the enzyme used in a luciferase-based reporter system, pPL2lux, harboring the listerial secA and hlyA promoters translationally fused to luxABCDE, overview
biotechnology
-
the enzyme and cyanine fluorescent protein are useful dual reporters for the quantitative analysis of the effects of n-dodecyltrimethylammonium bromide on whole cells and intracellular proteins of Pseudomonas putida
medicine
-
expression in Staphylococcus aureus Xen29. In the absence of antibiotics, staphylococcal bioluminescence increases over time until a maximum after ca. 6 h of growth, and subsequently decreases to the detection threshold after 24 h of growth. Up to minimal inhibitory concentrations of the antibiotics vancomycin, ciprofloxacin, erythromycin or chloramphenicol, bioluminescence increases according to a similar pattern up to 6 h of growth, but after 24 h, bioluminescence is higher than in the absence of antibiotics. Antibiotic pressure impacts the relation between bioluminescence per organism and bioluminescence. Under antibiotic pressure, bioluminescence is not controlled by luxA expression but by cofactors impacting the bacterial metabolic activity
medicine
transient and stable transfection of human kidney, breast cancer, and colorectal cancer cell lines by a codon optimized lux expression cassette using viral 2A elements as linker regions. The expression product produces autobioluminescent phenotypes in all cell lines tested without the induction of cytotoxicity and allows for repeated interrogation of populations and self-directed control of bioluminescent activation with detection limits and EC50 values similar to traditional reporter systems
molecular biology
-
enzyme can be used to monitor changes in gene expression as a reporter system in slow-growing mycobacteria, i.e. Mycobacterium tuberculosis strain H37Ra, determination of recombinant enzyme decay rate
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
molecular biology
-
the enzyme is used as a reporter system tool for analysis of promoter and gene expression activity, overview
-
synthesis
upon expression in Bacillus subtilis cells, luciferase is substantially more thermostable than in Escherichia coli. Thermal inactivation in Bacillus subtilis at 48.5#°C behaves as a first-order reaction. In Escherichia coli, the first order rate constant of the thermal inactivation exceeds that observed in B. subtilis cells 2.9 times. In dnaK-negative strains of Bacillus subtilis, both the rates of thermal inactivation and the efficiency of refolding are similar to that observed in wild-type strains
synthesis
upon expression in Bacillus subtilis cells, luciferase is substantially more thermostable than in Escherichia coli. Thermal inactivation in the cells of Escherichia coli and Bacillus subtilis may be described by first and third order kinetics, respectively. In dnaK-negative strains of Bacillus subtilis, both the rates of thermal inactivation and the efficiency of refolding are similar to that observed in wild-type strains