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1,3-dinitrobenzene + NADH + H+
? + NAD+
-
10.6% activity compared to FMN
-
-
?
1,4-benzoquinone + NADH + H+
1,4-benzoquinol + NAD+
-
18.6% activity compared to FMN
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
3-nitrophenol + NADH + H+
? + NAD+
-
8.95% activity compared to FMN
-
-
?
4-nitroacetophenone + NADH + H+
? + NAD+
-
17.9% activity compared to FMN
-
-
?
4-nitroaniline + NADH + H+
? + NAD+
-
4.91% activity compared to FMN
-
-
?
4-nitrobenzoate + NADH + H+
? + NAD+
-
21.2% activity compared to FMN
-
-
?
4-nitrophenol + NADH + H+
? + NAD+
-
8.07% activity compared to FMN
-
-
?
4-nitrotoluene + NADH + H+
? + NAD+
-
8.83% activity compared to FMN
-
-
?
FAD + NAD(P)H
FADH2 + NAD(P)+
FAD + NADH + H+
FADH2 + NAD+
-
58.1% activity compared to FMN
-
-
?
FAD + NADPH
FADH2 + NADP+
FAD + NADPH + H+
FADH2 + NADP+
FAD + NADPH + H+
reduced FAD + NADP+
FMN + NAD(P)H
FMNH2 + NAD(P)+
FMN + NADH
FMNH2 + NADP+
-
preference for NADPH over NADH, rate of reduction is 80 times faster with NADPH
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN + NADPH
FMNH2 + NADP+
FMN + NADPH
FMNH2 + NADP+ + H+
-
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
FMN + NADPH + H+
reduced FMN + NADP+
FMNH2 + NADP+
FMN + NADPH + H+
galactoflavin + NADPH
reduced galactoflavin + NADP+
lumiflavin + NADH + H+
reduced lumiflavin + NAD+
-
14.1% activity compared to FMN
-
-
?
lumiflavin + NADPH + H+
reduced lumiflavin + NADP+
menadione + NADH + H+
menadiol + NAD+
-
19.0% activity compared to FMN
-
-
?
methyl-4-nitrobenzoate + NADH + H+
? + NAD+
-
10.7% activity compared to FMN
-
-
?
methylene blue + NADH + H+
reduced methylene blue + NAD+
-
29.0% activity compared to FMN
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
nitrofurantoin + NADH + H+
? + NAD+
-
10.1% activity compared to FMN
-
-
?
nitrofurazone + NADH + H+
reduced nitrofurazone + NAD+
-
13.5% activity compared to FMN
-
-
?
nitrofurazone + NADPH + 4 H+
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+
-
-
-
-
?
oxidized methylene blue + NADPH + H+
reduced methylene blue + NADP+
-
-
-
-
?
oxidized riboflavin + NADPH + H+
reduced riboflavin + NADP+
reduced 2-thioFMN + NAD+
?
-
-
-
-
r
riboflavin + NAD(P)H
reduced riboflavin + NAD(P)+
-
-
-
-
r
riboflavin + NAD(P)H
reduced riboflavin + NADP+
-
redox potential of the irreversible reductive half-reaction
-
-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
29.0% activity compared to FMN
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
riboflavin + NADPH + H+
reduced riboflavin + NADP+
riboflavin-5-phosphate + NADH + H+
reduced FMN + NAD+
additional information
?
-
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
15.4% activity compared to FMN
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
15.4% activity compared to FMN
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
8.48% activity compared to FMN
-
-
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
8.48% activity compared to FMN
-
-
?
FAD + NAD(P)H
FADH2 + NAD(P)+
-
-
-
-
r
FAD + NAD(P)H
FADH2 + NAD(P)+
-
-
-
-
r
FAD + NADPH
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH
FADH2 + NADP+
-
-
-
-
r
FAD + NADPH
FADH2 + NADP+
-
-
-
-
r
FAD + NADPH
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
-
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
-
-
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
-
specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
the enzyme (BLVRB) binds its coenzyme NADPH 500fold more tightly than its substrate FAD
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
XP_020138941.1
-
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
-
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
-
-
-
r
FAD + NADPH + H+
FADH2 + NADP+
-
-
-
?
FAD + NADPH + H+
reduced FAD + NADP+
-
-
-
-
?
FAD + NADPH + H+
reduced FAD + NADP+
-
-
-
-
?
FMN + NAD(P)H
FMNH2 + NAD(P)+
-
-
-
-
r
FMN + NAD(P)H
FMNH2 + NAD(P)+
-
-
-
-
r
FMN + NAD(P)H
FMNH2 + NAD(P)+
-
-
-
-
r
FMN + NADH
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
-
?
FMN + NADH + H+
FMNH2 + NAD+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
preference for NADPH over NADH, rate of reduction is 80 times faster with NADPH
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
r
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
r
FMN + NADPH
FMNH2 + NADP+
-
reaction may be coupled with luciferase for bioluminescence
-
-
?
FMN + NADPH
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
203% activity compared to NAD+
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
203% activity compared to NAD+
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
-
-
?
FMN + NADPH + H+
reduced FMN + NADP+
-
-
-
-
?
FMN + NADPH + H+
reduced FMN + NADP+
-
-
-
-
?
FMNH2 + NADP+
FMN + NADPH + H+
-
-
-
r
FMNH2 + NADP+
FMN + NADPH + H+
-
-
-
r
galactoflavin + NADPH
reduced galactoflavin + NADP+
-
-
-
-
?
galactoflavin + NADPH
reduced galactoflavin + NADP+
-
-
-
-
?
lumiflavin + NADPH + H+
reduced lumiflavin + NADP+
-
-
-
-
?
lumiflavin + NADPH + H+
reduced lumiflavin + NADP+
-
-
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
23.0% activity compared to FMN
-
-
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
23.0% activity compared to FMN
-
-
?
nitrofurazone + NADPH + 4 H+
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
-
-
-
-
?
nitrofurazone + NADPH + 4 H+
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
-
-
-
-
?
oxidized riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
?
oxidized riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
-
-
-
r
riboflavin + NADPH
reduced riboflavin + NADP+
-
i.e. FMN
i.e. FMNH2
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
redox potential and equilibria in the reversible reductive half-reaction
-
-
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
-
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
-
-
?
riboflavin-5-phosphate + NADH + H+
reduced FMN + NAD+
-
-
-
-
r
riboflavin-5-phosphate + NADH + H+
reduced FMN + NAD+
-
-
-
-
r
additional information
?
-
-
enzyme additionally has azoreductase activity cleaving the -N=N- bond in azo dyes
-
-
?
additional information
?
-
-
the enzyme reduces both nitrofurazone and FMN effectively, it is bifunctional as flavin reductase and nitroreductase. Two different FMN molecules are involved in the FMN reduction process: FMN tightly associated to the enzyme as prosthetic group and FMN as a substrate. The enzyme is also active with FAD, riboflavin, and lumiflavin, the two latter give the highest activity
-
-
?
additional information
?
-
-
the enzyme reduces both nitrofurazone and FMN effectively, it is bifunctional as flavin reductase and nitroreductase. Two different FMN molecules are involved in the FMN reduction process: FMN tightly associated to the enzyme as prosthetic group and FMN as a substrate. The enzyme is also active with FAD, riboflavin, and lumiflavin, the two latter give the highest activity
-
-
?
additional information
?
-
-
bifunctional enzyme flavin reductase (NADPH)/biliverdin-IXbeta reductase
-
-
?
additional information
?
-
-
prefers NADPH over NADH
-
-
?
additional information
?
-
-
prefers NADPH over NADH
-
-
?
additional information
?
-
-
the enzyme is also active with FMN and NADH, cf. EC 1.5.1.36
-
-
?
additional information
?
-
-
the enzyme is also active with FMN and NADH, cf. EC 1.5.1.36
-
-
?
additional information
?
-
-
no catalytic activity is detected with NADH
-
-
?
additional information
?
-
significant reduction of NADP+ by rFlaR refolded in the presence Fe2+. Fe2+ is the electron donor in the rFlaR-NADP+ reductase activity
-
-
-
additional information
?
-
FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction
-
-
?
additional information
?
-
-
FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction
-
-
?
additional information
?
-
FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction
-
-
?
additional information
?
-
-
enzyme transfers reduced riboflavin 5'-phosphate to luciferase by direct channeling in vitro and in vivo, formation of donor-acceptor enzyme complex
-
-
?
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0.007
2-thioFMN
-
enzyme reconstituted from apoenzyme and 2-thioFMN
0.053
oxidized riboflavin
pH 7.5, 25°C
additional information
additional information
-
0.0036
FAD
-
-
0.236
FAD
XP_020138941.1
pH and temperature not specified in the publication
0.000016
FMN
-
25°C, single-enzyme assay
0.00013
FMN
-
25°C, enzyme in complex with monooxygenase SsuD, presence of octanesulfonate
0.00013
FMN
-
presence of 1.05 mM O2
0.0009
FMN
-
coupled oxidoreductase-luciferase assay, kcat/Km = 73/(M*min), in 100 mM Na+/K+ phosphate buffer with 100 mM NaCl, pH 7.0, 1 microM Fre oxidoreductase, 10 microM decanal, 10 microM NADPH, 5 microM luciferase
0.002
FMN
-
mutant enzyme E99K, in 50 mM phosphate buffer, at pH 7.0, at 23°C
0.0047
FMN
-
pH 7.0, 23°C, recombinant enzyme
0.0058
FMN
-
flavin reductase P R203A
0.0069
FMN
-
native flavin reductase P
0.008
FMN
-
native enzyme, at 23°C in 50 mM phosphate buffer, pH 7.0
0.021
FMN
-
recombinant fusion protein, pH 7.0, 23°C
0.05
FMN
-
pH and temperature not specified in the publication
0.072
FMN
-
enzyme fused to luciferase, at 23°C in 50 mM phosphate buffer, pH 7.0
14.2
FMN
-
in the presence of NADPH
0.208
NADH
-
-
0.5
NADH
-
in the presence of FMN
0.000019
NADPH
-
presence of 1.05 mM O2
0.00007
NADPH
-
mutant enzyme E99K, in 50 mM phosphate buffer, at pH 7.0, at 23°C
0.00085
NADPH
-
nitrofurazone as electron acceptor
0.002
NADPH
-
pH and temperature not specified in the publication
0.003
NADPH
-
enzyme reconstituted from apoenzyme and 2-thioFMN
0.0035
NADPH
-
FMN as electron accceptor
0.0039
NADPH
-
pH 7.0, 23°C, recombinant enzyme, with FMN
0.0054
NADPH
-
25°C, single-enzyme assay
0.009
NADPH
-
wild type enzyme, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
0.01
NADPH
-
mutant enzyme R225A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
0.0109
NADPH
-
with FMN, pH 7.5, 30°C, recombinant enzyme
0.016
NADPH
-
mutant enzyme R133A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
0.0184
NADPH
-
with FAD, pH 7.5, 30°C, recombinant enzyme
0.02
NADPH
-
native enzyme, at 23°C in 50 mM phosphate buffer, pH 7.0
0.021
NADPH
-
native flavin reductase P
0.032
NADPH
-
FAD as electron acceptor
0.034
NADPH
-
mutant enzyme N134A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
0.048
NADPH
-
recombinant fusion protein, pH 7.0, 23°C
0.05
NADPH
-
at a saturating concentration of FMN
0.31
NADPH
-
enzyme fused to luciferase, at 23°C in 50 mM phosphate buffer, pH 7.0
0.55
NADPH
-
pH 7.5, 37°C
0.71
NADPH
-
flavin reductase P R203A
0.0013
riboflavin
-
coupled oxidoreductase-luciferase assay, kcat/Km = 1257/(M*min), in 100 mM Na+/K+ phosphate buffer with 100 mM NaCl, pH 7.0, 1 microM Fre oxidoreductase, 10 microM decanal, 10 microM NADPH, 5 microM luciferase, riboflavin is favoured by Fre oxidoreductase but a poor substrate for bacterial luciferase
additional information
additional information
-
substrate and cofactor binding, reaction kinetics
-
additional information
additional information
-
substrate and cofactor binding, reaction kinetics
-
additional information
additional information
-
Km-value of both NADPH and FMN gradually decreases at increasing concentrations of oxygen, with 0.000104 and 0.000019 mM as the upper limits for Km of FMN and NADPH, resp.
-
additional information
additional information
-
enzyme kinetic analysis, overview
-
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malfunction
a flaR mutant is highly susceptible to H2O2 compared to its wild-type and complemented strains, suggesting a role for FlaR in pneumococcal oxidative stress resistance. The flaR mutant demonstrates significantly decreased mice mortality following intraperitoneal infection. A lack of FlaR does not affect the extent of phagocytosis by primary mouse peritoneal macrophages but reduces adhesion to A549 cells compared to wild-type and complemented strains
evolution
-
analysis of evolutionary or molecular mechanism of divergence of the nitroreductase/flavin reductase family, overview. The enzyme is similar to NfsA from Escherichia coli, overview
evolution
a position 15 A away from the active site within human biliverdin reductase B (T164) is inherently dynamic and can be mutated to control global micro-millisecond motions and function. By comparing the inherent dynamics through nuclear magnetic resonance (NMR) relaxation approaches of evolutionarily distinct biliverdin reductase B homologues and by applying Relaxation And Single Site Multiple Mutations (RASSMM) approach that monitors both the functional and dynamic effects of multiple mutations to the single T164 site, it is discovered that the most dramatic mutagenic effects coincide with evolutionary changes and these modulate coenzyme binding
evolution
in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning
evolution
in many luminous species (ie, Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning
evolution
in many luminous species (ie, Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning
evolution
most BLVRB enzymes have an arginine at either residue 14 or residue 78 (human numbering), although a subset maintain an arginine at both sites. In primates, the two substitutions are made on the same branch separating the common ancestor of the Simiiformes (apes, new and old-world monkeys) with the common ancestor of the Haplorhini (i.e., after the split from the common ancestor with the tarsier). This suggests possible adaptive coevolution at these two sites and adjusting the location of this arginine may serve to fine-tune coenzyme binding in BLVRB enzymes
evolution
the flavin reductase DNA sequence of the TIGR4 strain is compared to 29 completely sequenced genomes of Streptococcus pneumoniae. All 29 genomes contain a highly similar locus to SP_RS 02775
evolution
the study elucidates the role of the evolutionarily changing biliverdin reductase (BBLVRB) active site that serves to modulate coenzyme release and shows that coenzyme release is coupled to substrate turnover
evolution
XP_020138941.1
the study elucidates the role of the evolutionarily changing biliverdin reductase (BBLVRB) active site that serves to modulate coenzyme release and shows that coenzyme release is coupled to substrate turnover
evolution
-
analysis of evolutionary or molecular mechanism of divergence of the nitroreductase/flavin reductase family, overview. The enzyme is similar to NfsA from Escherichia coli, overview
-
metabolism
-
the flavin reductase couples with dibenzothiophene and dibenzothiophene sulfone monooxygenase in the thermophilic dibenzothiophene (DBT)-desulfurizing bacterium, the flavin reductase exhibits flavin reductase and nitroreductase activities
metabolism
-
CysJ functions as a specific partner of the YcbX molybdoenzyme and provides the reducing equivalents needed for the detoxification reaction at the YcbX molybdocenter
metabolism
Trichomonas vaginalis has two different enzymatic pathways to remove intracellular oxygen, i.e. NADH oxidase, which is inhibited by metronidazole, and flavin reductase
metabolism
heme degradation enzyme biliverdin IXbeta reductase is required for stem cell glutamine metabolism
metabolism
in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate
metabolism
in many luminous species (ie, Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate
metabolism
in many luminous species (ie, Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate
metabolism
-
the flavin reductase couples with dibenzothiophene and dibenzothiophene sulfone monooxygenase in the thermophilic dibenzothiophene (DBT)-desulfurizing bacterium, the flavin reductase exhibits flavin reductase and nitroreductase activities
-
metabolism
-
Trichomonas vaginalis has two different enzymatic pathways to remove intracellular oxygen, i.e. NADH oxidase, which is inhibited by metronidazole, and flavin reductase
-
physiological function
-
provides reducing equivalents required to drive the luciferase genes in Escherichia coli but is not coupled to luciferase
physiological function
-
CysJ is involved in 6-N-hydroxylaminopurine resistance
physiological function
regarding all flavin reductase enzymes in Trichomonas vaginalis, FR1 is responsible for the flavin reductase activity. Hydrogen peroxide is the main if not the single product of FR1. FR1 displays a 10 to 20fold higher affinity to FMN than enzymes FR5 and FR6. Also the affinity of FR1 to FAD is at least 10fold higher than observed with FR5 and FR6 but the Vmax is considerably lower (roughly 33% of the Vmax for FMN). In contrast, FR5 and FR6 display higher affinity for riboflavin than FR1, which is inhibited by riboflavin
physiological function
flavin reductase contributes to pneumococcal virulence by protecting from oxidative stress and mediating adhesion and elicits protection against pneumococcal challenge, role for FlaR in pneumococcal oxidative stress resistance. FlaR involvement in virulence i.e. adhesion to host cells, mechanism, overview
physiological function
the enzyme is a critical players in cellular redox regulation
physiological function
-
regarding all flavin reductase enzymes in Trichomonas vaginalis, FR1 is responsible for the flavin reductase activity. Hydrogen peroxide is the main if not the single product of FR1. FR1 displays a 10 to 20fold higher affinity to FMN than enzymes FR5 and FR6. Also the affinity of FR1 to FAD is at least 10fold higher than observed with FR5 and FR6 but the Vmax is considerably lower (roughly 33% of the Vmax for FMN). In contrast, FR5 and FR6 display higher affinity for riboflavin than FR1, which is inhibited by riboflavin
-
additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases
additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases
additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases
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