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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
decanal + FMNH + O2
decanoic acid + FMN + H2O + light
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 + 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
fatty aldehyde + FMNH2 + O2
fatty acid + FMN + H2O + hn
-
-
-
-
ir
FMNH + O2
FMN + H2O2
-
-
-
-
?
hexachlorethane + e-
tetrachlorethylene + Cl-
-
-
-
-
?
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
?
-
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
-
-
?
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 + 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
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
-
-
-
-
?
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 + FMNH2 + O2
dodecanoate + FMN + H2O + hn
-
-
-
-
?
dodecanal + FMNH2 + O2
dodecanoate + FMN + H2O + hn
-
-
-
-
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
-
-
-
?
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
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
-
-
-
-
?
tetradecanal + FMNH2 + O2
tetradecanoate + FMN + H2O + hn
-
-
-
-
ir
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
-
-
?
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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
0.0004 - 0.0008
FMNH
-
-
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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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
-
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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243
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2006
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Active site hydrophobicity is critical to the bioluminescence activity of Vibrio harveyi luciferase
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2005
Vibrio harveyi
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Probing the functionalities of alphaGlu328 and alphaAla74 of Vibrio harveyi luciferase by site-directed mutagenesis and chemical rescue
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2005
Vibrio harveyi
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2008
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Fre Is the Major Flavin Reductase Supporting Bioluminescence from Vibrio harveyi Luciferase in Escherichia coli
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2009
Vibrio harveyi
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Crystal structure of the bacterial luciferase/flavin complex provides insight into the function of the beta subunit
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2009
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Two lysine residues in the bacterial luciferase mobile loop stabilize reaction intermediates
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2009
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Ke, D.; Tu, S.C.
Activities, kinetics and emission spectra of bacterial luciferase-fluorescent protein fusion enzymes
Photochem. Photobiol.
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2011
Vibrio harveyi
brenda
Kim, T.; Spiegel, D.
Serendipitous discovery of two highly selective inhibitors of bacterial luciferase
Tetrahedron
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7692-7698
2013
Vibrio harveyi, Vibrio harveyi BB120
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brenda
Born, Y.; Fieseler, L.; Thoeny, V.; Leimer, N.; Duffy, B.; Loessner, M.J.
Engineering of bacteriophages Y2-dpoL1-C and Y2-luxAB for efficient control and rapid detection of the fire blight pathogen, Erwinia amylovora
Appl. Environ. Microbiol.
83
e00341
2017
Vibrio harveyi
brenda
Melkina, O.E.; Goryanin, I.I.; Manukhov, I.V.; Baranova, A.V.; Kolb, V.A.; Svetlov, M.S.; Zavilgelsky, G.B.
Trigger factor assists the refolding of heterodimeric but not monomeric luciferases
Biochemistry (Moscow)
79
62-68
2014
Photobacterium leiognathi, Photobacterium leiognathi (P07740 and P07739), Vibrio harveyi (P07740 and P07739), Aliivibrio fischeri (P19907 and P19908), Aliivibrio fischeri MJ-1 (P19907 and P19908)
brenda
Brodl, E.; Ivkovic, J.; Tabib, C.R.; Breinbauer, R.; Macheroux, P.
Synthesis of alpha,beta-unsaturated aldehydes as potential substrates for bacterial luciferases
Bioorg. Med. Chem.
25
1487-1495
2017
Aliivibrio fischeri, Photobacterium leiognathi, Vibrio harveyi, Vibrio harveyi ATCC 14126, Aliivibrio fischeri ATCC 7744
brenda
Jiang, T.; Wang, W.; Wu, X.; Wu, W.; Bai, H.; Ma, Z.; Shen, Y.; Yang, K.; Li, M.
Discovery of new substrates for LuxAB bacterial bioluminescence
Chem. Biol. Drug Des.
88
197-208
2016
Vibrio harveyi
brenda
Tinikul, R.; Lawan, N.; Akeratchatapan, N.; Pimviriyakul, P.; Chinantuya, W.; Suadee, C.; Sucharitakul, J.; Chenprakhon, P.; Ballou, D.P.; Entsch, B.; Chaiyen, P.
Protonation status and control mechanism of flavin-oxygen intermediates in the reaction of bacterial luciferase
FEBS J.
288
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2021
Vibrio harveyi (P07740 and P07739)
brenda
Nemtseva, E.V.; Gulnov, D.V.; Gerasimova, M.A.; Sukovatyi, L.A.; Burakova, L.P.; Karuzina, N.E.; Melnik, B.S.; Kratasyuk, V.A.
Bacterial luciferases from Vibrio harveyi and Photobacterium leiognathi demonstrate different conformational stability as detected by time-resolved fluorescence spectroscopy
Int. J. Mol. Sci.
22
14994
2021
Vibrio harveyi (P07740 and P07739), Photobacterium leiognathi (P09140 and P09141)
brenda
Lawan, N.; Tinikul, R.; Surawatanawong, P.; Mulholland, A.J.; Chaiyen, P.
QM/MM molecular modeling reveals mechanism insights into flavin peroxide formation in bacterial buciferase
J. Chem. Inf. Model.
62
399-411
2022
Vibrio harveyi (P07740 and P07739)
brenda