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Information on EC 1.5.1.30 - flavin reductase (NADPH)
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1.5.1.30 flavin reductase (NADPH)IUBMB Comments
The enzyme reduces riboflavin, and, less efficiently, FMN and FAD. NADH is oxidized less efficiently than NADPH.
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Word Map
- 1.5.1.30
- monooxygenase
- mononucleotide
- harveyi
-
flavin-dependent
- fmnh2
- fischeri
- dibenzothiophene
-
desulfurization
- halogenases
-
oxygen-insensitive
-
nadh:flavin
- nitroreductases
-
biodesulfurization
-
leiognathi
-
fadh2-dependent
-
single-enzyme
- 2-hydroxybiphenyl
The enzyme appears in viruses and cellular organisms
Synonyms
flavin reductase, flavin oxidoreductase, nadph-dependent diaphorase, nadph-flavin reductase, flavin reductase p, nadph:fmn oxidoreductase, nfra1, nadph-specific flavin reductase, nadph:flavin oxidoreductase, ipa-43d, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
azoreductase
AZRü
flavin reductase
flavin reductase 1
FR1
Frb
Frd188
frd2
Fre-1
FRP
HpaC
ipa-43d
NAD(P)H-dependent H2O2-forming flavin reductase
NADPH-flavin reductase
NADPH-FMN reductase
NADPH-nitrofurazone reductase
NADPH:flavin oxidoreductase
NfrA1
nitro/flavin reductase
TVAG_517010
additional information
azoreductase
-
flavodoxin that also functions as nitroreductase and flavin mononucleotide reductase
azoreductase
-
flavodoxin that also functions as nitroreductase and flavin mononucleotide reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
-
-
-
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
ping-pong mechanism
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
bi-bi ternary mechanism, i.e. both FMN and NADPH must bind to the active site before catalysis can occur
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
binding of FMN by apoenzyme is noncooperative, exothermic and primarily enthalpy driven with significant conformational changes in enzyme upon binding. The kinetically deduced ping-pong mechanism is supported by measurement of binding affinities of the oxidized and reduced FMN cofoactors
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
FRP:luciferase coupled reaction can utilize reduced flavin by both free diffusion and direct transfer
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
single-enzyme kinetic assay, SsuE follows ordered sequential mechanism with NADPH as the first substrate to bind and NADP+ as the last product to leave. In presence of monooxygenase SsuD and octanesulfonate mechanism is altered to rapid equilibrium ordered mechanism, and Km-value for FMN increases 10fold
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the nicotinamide of NAD+ stacks the isoalloxazine ring of FMN so that NADH can directly transfer hydride. The bound NADP+ also has a compact conformation but is bound in a reverse direction, which is not suitable for hydride transfer
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the enzyme catalysis obeys the ping-pong Bi-Bi kinetic mechanism with substrate FMN as well as substrate nitrofurazone, but upon coupling with the bioluminescent reaction of luciferase, it changes to the sequential mechanism
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the nicotinamide of NAD+ stacks the isoalloxazine ring of FMN so that NADH can directly transfer hydride. The bound NADP+ also has a compact conformation but is bound in a reverse direction, which is not suitable for hydride transfer
-
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
the enzyme catalysis obeys the ping-pong Bi-Bi kinetic mechanism with substrate FMN as well as substrate nitrofurazone, but upon coupling with the bioluminescent reaction of luciferase, it changes to the sequential mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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SYSTEMATIC NAME
IUBMB Comments
reduced-riboflavin:NADP+ oxidoreductase
The enzyme reduces riboflavin, and, less efficiently, FMN and FAD. NADH is oxidized less efficiently than NADPH.
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CAS REGISTRY NUMBER
COMMENTARY
56626-29-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
?
4-nitroacetophenone + NADH + H+
? + NAD+
-
17.9% activity compared to FMN
-
?
4-nitrobenzoate + NADH + H+
? + NAD+
-
21.2% activity compared to FMN
-
?
FMN + NADH
FMNH2 + NADP+
-
preference for NADPH over NADH, rate of reduction is 80 times faster with NADPH
-
?
lumiflavin + NADH + H+
reduced lumiflavin + NAD+
-
14.1% activity compared to FMN
-
?
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
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+
-
-
-
?
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
-
?
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 + NADPH + H+
FADH2 + NADP+
-
specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
-
?
FMN + NADPH
FMNH2 + NADP+
-
preference for NADPH over NADH, rate of reduction is 80 times faster with NADPH
-
?
FMN + NADPH
FMNH2 + NADP+
-
reaction may be coupled with luciferase for bioluminescence
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
203% activity compared to NAD+
-
?
FMN + NADPH + H+
FMNH2 + NADP+
-
specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
-
?
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+
-
specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
-
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
redox potential and equilibria in the reversible reductive half-reaction
-
?
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
?
-
-
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
?
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FMN + NADPH + H+
FMNH2 + NADP+
-
203% activity compared to NAD+
-
-
?
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
-
contains one FMN cofactor per monomer, the FMN cofactor of FRPVh can be replaced by 2-thioFMN to yield a catalytically active reconstituted reductase
FMN
-
contains one FMN cofactor per monomer, the FMN cofactor of FRPVh can be replaced by 2-thioFMN to yield a catalytically active reconstituted reductase
FMN
-
the presence of exogenously added FMN is necessary for activity
FMN
-
tightly associated to, 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
NADPH
-
the FMN reductase activity is highly specific for NADPH, and the activity with NADH is 10% of that with NADPH
additional information
FR1 displays only 3% activity when NADH is added instead of NADPH
-
additional information
-
FR1 displays only 3% activity when NADH is added instead of NADPH
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Fe2+, Fe3+, Mg2+, and Ca2+ do not affect the enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Amaranth
-
the presence of 50 mM amaranth reduces the NADPH oxidation rate 2.6fold
lumichrome
competitive inhibitor against FMN and a mixed inhibitor of NADPH
mesobiliverdin XIIIa
competitive kinetics with FMN and mixed inhibition kinetics with NADPH
NEM
-
when the enzyme is preincubated with NEM and NADH in the absence of FMN
Ponceau BS
-
the presence of 50 mM Ponceau BS reduces the NADPH oxidation rate 3.7fold
riboflavin
FR1 inhibition by possibly either by the semiquinone or the fully reduced form
additional information
-
with 1 mM ethylenediaminetetraacetic acid 99.8% activity, with 1 mM 2,2'-bipyridyl 81.8% activity
-
NADP+
-
0.1 mM, about 50% inhibition at no inhibition by NAD+ at pH 7.5, 12% inhibition at pH 4.8
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme coexpression with gene dcs-1 is induced by heat shock
-
additional information
enzyme coexpression with gene dcs-1 is induced by heat shock
-
additional information
-
enzyme coexpression with gene dcs-1 is induced by heat shock
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma of Lung
Identification of Up- and Down-Regulated Proteins in Pemetrexed-Resistant Human Lung Adenocarcinoma: Flavin Reductase and Calreticulin Play Key Roles in the Development of Pemetrexed-Associated Resistance.
Amyotrophic Lateral Sclerosis
Partial loss of NADPH-diaphorase/nitric oxide synthase-complex in amyotrophic lateral sclerosis and human type-II myofiber atrophy.
Leukemia
Purification of an NADPH-dependent diaphorase from membrane of DMSO-induced differentiated human promyelocytic leukemia HL-60 cells.
Methemoglobinemia
Flavin reductase: sequence of cDNA from bovine liver and tissue distribution.
Whooping Cough
[Cloning and analysis of genes encoding 2-naphthoate monooxygenase and NADH:flavin oxidoreductase]
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00013
FMN
-
25°C, enzyme in complex with monooxygenase SsuD, presence of octanesulfonate
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
0.072
FMN
-
enzyme fused to luciferase, at 23°C in 50 mM phosphate buffer, pH 7.0
0.00007
NADPH
-
mutant enzyme E99K, in 50 mM phosphate buffer, at pH 7.0, at 23°C
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
0.016
NADPH
-
mutant enzyme R133A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
0.034
NADPH
-
mutant enzyme N134A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
0.31
NADPH
-
enzyme fused to luciferase, at 23°C in 50 mM phosphate buffer, pH 7.0
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
FMN
-
25°C, enzyme in complex with monooxygenase SsuD, presence of octanesulfonate
11.7
FMN
-
enzyme fused to luciferase, at 23°C in 50 mM phosphate buffer, pH 7.0
5.2
NADPH
-
mutant enzyme N134A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
9.2
NADPH
-
mutant enzyme R133A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
19.2
NADPH
-
mutant enzyme R225A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
23.8
NADPH
-
wild type enzyme, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.021
riboflavin
-
coupled oxidoreductase-luciferase assay, 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
0.0012
FMN
-
coupled oxidoreductase-luciferase assay, 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
12
NADPH
-
mutant enzyme R15A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
25
NADPH
-
mutant enzyme K167A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
150
NADPH
-
mutant enzyme N134A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
570
NADPH
-
mutant enzyme R133A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
2000
NADPH
-
mutant enzyme R225A, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
2670
NADPH
-
wild type enzyme, in 20 mM N-tris[hydroxymethyl]methyl-3-aminopropanesulfonic acid buffer, pH 7.0, at 22°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0035
NADPH
-
25°C, enzyme in complex with monooxygenase SsuD, presence of octanesulfonate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
-
maximum activity at pH 6.0, more than 80% activity at pH 5.5, 6.5, and 7.0, about 75% activity at pH 7.5, about 30% activity at pH 8.5, less than 20% activity at pH 9-9.5, less than 10% activity at pH 4, 4.5, and 10, pH 4.0-6.0 citrate-phosphate buffer, pH 6.0-7.5 potassium-phosphate buffer, pH 7.5-8.5 Tris-HCl buffer, pH 8.5-10.0 glycine-NaOH buffer
4.5 - 8
-
pH 4.5: about 85% of maximal activity, pH 8.0: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 55
-
maxiumum activity at 50°C, about 90% activity at 45°C, about 80% at 40 and 55°C, about 50-60% activity at 35 and 60°C, about 40% activity at 30°C, about 30% activity at 25°C, about 20% activity at 20 and 65°C, no activity at 70°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
enzyme SsuE is part of alkanesulfonate monooxygenase system, together with a monooxygenase enzyme SsuD
-
-
brenda
bifunctional enzyme biliverdin reductase/flavin reductase (NADPH)
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
genes fre-1 and dcs-1 are coordinately expressed through worm development
brenda
additional information
analysis of enzyme FR1 expression in metronidazole-susceptible isolates C1, G3, JH31A and Tv2: the highly metronidazole-resistant cell line of strain C1, C1res, and the clinical isolate B7268 lack detectable FRs. The residual FR activity found in CDC085 and LA1 likely results from alternative FRs that are highly expressed
brenda
additional information
-
analysis of enzyme FR1 expression in metronidazole-susceptible isolates C1, G3, JH31A and Tv2: the highly metronidazole-resistant cell line of strain C1, C1res, and the clinical isolate B7268 lack detectable FRs. The residual FR activity found in CDC085 and LA1 likely results from alternative FRs that are highly expressed
brenda
additional information
-
analysis of enzyme FR1 expression in metronidazole-susceptible isolates C1, G3, JH31A and Tv2: the highly metronidazole-resistant cell line of strain C1, C1res, and the clinical isolate B7268 lack detectable FRs. The residual FR activity found in CDC085 and LA1 likely results from alternative FRs that are highly expressed
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
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
-
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
-
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
-
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
Show AA Sequence and Transmembrane Helices (326 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Shewanella oneidensis (strain MR-1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22000
26300
28000
28400
-
4 * 28400, dynamic light scattering, ArsH in solution at room temperature does exist predominantly in the tetrameric form
40000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotetramer
monomer
tetramer
dimer
-
dimerization of native enzyme and apoenzyme, equilibrium ultracentrifugation
homodimer
-
2 * 28320, sequence calculation, 2 * 28000, recombinant untagged enzyme, SDS-PAGE
homodimer
-
2 * 28320, sequence calculation, 2 * 28000, recombinant untagged enzyme, SDS-PAGE
tetramer
-
4 * 28400, dynamic light scattering, ArsH in solution at room temperature does exist predominantly in the tetrameric form
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method, using 0.2 M calcium chloride and 20% (w/v) polyethylene glycol 3350
-
in NAD(P)(+)-free, NAD(+)-bound, and NADP(+)-bound states. The nicotinamide of NAD+ stacks the isoalloxazine ring of FMN so that NADH can directly transfer hydride. The bound NADP+ also has a compact conformation but is bound in a reverse direction, which is not suitable for hydride transfer
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L114M/L165M
-
mutant created to obtain selenomethionine-containing enzyme for crystallization. Activity of mutant is similar to wild-type, circular dichroism spectra identical to wiil-type
E99K
-
the mutation destabilizes the dimer and has an enhanced subunit dissociation as evident from a 44fold higher Kd for the monomer-dimer equilibrium
K167A
-
the mutant has apparently greatly increased Km and reduced kcat/Km for NADPH
R15A
-
the mutant has apparently greatly increased Km and reduced kcat/Km for NADPH
R203A
additional information
R203A
-
decrease of NADPH binding potential, critical role of Arg203 in the specific recognition and binding of NADPH
R203A
-
site-directed mutagenesis, no reversibility of the reduction of FMN, the half-reaction
additional information
-
improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd2, strain 5-5(frd2) and deletion strains 5-5DELTAfrd2 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutant 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd2) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview
additional information
-
improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd2, strain 5-5(frd2) and deletion strains 5-5DELTAfrd2 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutant 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd2) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview
additional information
-
Fre oxidoreductase deletion strain shows 99% reduced bioluminescence in coupled assay with luciferase
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 12
-
about 80% activity retained after 24 h incubation at pH 2.0-3.5, 90 to less than 100% at pH 4.0-5.5 and pH 8.0-12.0, 100% at pH 6.0-7.5, pH 4.0-6.0 citrate-phosphate buffer, pH 6.0-7.5 potassium-phosphate buffer, pH 7.5-8.5 Tris-HCl buffer, pH 8.5-10.0 glycine-NaOH buffer
699057
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
boiling of the enzyme leads to complete loss of the FMN reductase activity
20 - 70
-
30 min incubation at 20°C retains 100% activity, more than 90% activity is retained at 25-45°C, about 80% at 50°C, about 50% at 55°C, about 20% at 60°C, about 10% at 65°C, no activity at 70°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cells harvested by centrifugation, washing twice and suspended in 50 mM Tris-HCl buffer, pH 8.0, with 1 mM dithiothreitol and 10% glycerol, cells disrupted with ultraoscillator (20 kHz), debris removed by centrifugation, enzyme purified from cell-free extracts with ÄKTA explorer, applied to Toyopearl DEAE-650 M column, equilibrated with 50 mM Tris-HCl buffer, pH 8.0, washed, proteins eluted with linear gradient of 0-0.5 M KCl, active fractions (at 0.15-0.2 M KCl) combined and concentrated by ultrafiltration (membrane filter YM-30), enzyme purified with HiLoad 16/60 Superdex 200, equilibrated with 50 mM Tris-HCl buffer, pH 8.0 with 0.15 M NaCl, elution with same buffer
-
crude lysate assay with briefly centrifuged cells, resuspended in B-PER bacterial protein extraction reagent, recombinant pZCFRE1 expression product is clarified by centrifugation and applied to a custom nickel affinity column, dialyzed into buffer containing 100 mM Na+/K+ phosphate and 100 mM NaCl, pH 7.0
-
HiTrap DEAE column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration
-
recombinant enzyme 23fold from Escherichia coli to homogeneity by dialysis, anion exchange chromatography, dialysis, two steps of Blue Sepharose affinity chromatography, and again dialysis
-
recombinant enzyme from Escherichia coli strain BL21(DE3) to over 90% purity, recombinant fusion protein from Escherichia coli strain JM109 to over 80% purity
-
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant wild-type and mutant enzyme from Escherichia coli to homogeneity
-
the flavin reductase-luciferase fusion protein is purified using DEAE-cellulose DE-52 column chromatography, DEAE-Sepharose column chromatography, and Superdex 200 gel filtration
-
ultracentrifugation, G-25 gel filtration, DEAE-Sepharose column chromatography, and Sephadex G25 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
frb gene inserted into plasmid pET21-a, introduced into Escherichia coli BL21 (DE3), cultivated at 30°C
-
gene frd2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant overexpression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene fre-1, DNA and amino acid sequence determination and analysis, transcribed as a bicistronic pre-mRNA together with gene dcs-1, encoding Hint-related 7meGMP-directed hydrolase DCS-1
gene frp, functional expression of the enzyme fused to yellow fluorescence protein YFP in a Vibrio harveyi strain lacking the frp gene, subcloning and expression in Escherichia coli strains JM109 and BL21(DE3), the yellow fluorescence protein YFP is a mutant of the green fluorescence protein GFP, with mutations S65G, V68L, S72A, and T203Y
-
gene ipa-43d, DNA and amino acid sequence determination and analysis, genetic structure and sequence comparison, recombinant overexpression in Escherichia coli J83
-
gene TVAG_517010, DNA and amino acid sequence determination and analysis, quantitative RT-PCR expression analysis of FR1 in metronidazole-susceptible isolates C1, G3, JH31A and Tv2 , re-introduction of FR1 into an aerobically-resistant strain, transfection of the highly metronidazole-resistant isolate B7268 with the FR1 gene restores metronidazole susceptibility
gene fre-1, DNA and amino acid sequence determination and analysis, transcribed as a bicistronic pre-mRNA together with gene dcs-1, encoding Hint-related 7meGMP-directed hydrolase DCS-1
-
gene fre-1, DNA and amino acid sequence determination and analysis, transcribed as a bicistronic pre-mRNA together with gene dcs-1, encoding Hint-related 7meGMP-directed hydrolase DCS-1
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
soluble denatured mutant enzyme E99K is mixed into 50fold volume of pre-cooled 50 mM phosphate buffer containing 0.1 M FMN and stirred on ice in the dark for 15 min for protein renaturation and the reconstitution of E99K holoenzyme
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yubisui, T.; Matsuki, T.; Takeshita, M.; Yoneyama, Y.
Characterization of the purified NADPH-flavin reductase of human erythrocytes
J. Biochem.
85
719-728
1979
Homo sapiens
brenda
Tang, C.K.; Jeffers, C.E.; Nichols, J.C.; Tu, S.C.
Flavin specificity and subunit interaction of Vibrio fischeri general NAD(P)H-flavin oxidoreductase FRG/FRase I
Arch. Biochem. Biophys.
392
110-116
2001
Aliivibrio fischeri
brenda
Lo, H.S.; Reeves, R.E.
Purification and properties of NADPH: flavin oxidoreductase from Entamoeba histolytica
Mol. Biochem. Parasitol.
2
23-30
1980
Entamoeba histolytica, Entamoeba histolytica NIH:200
brenda
Lei, B.; Liu, M.; Huang, S.; Tu, S.C.
Vibrio harveyi NADPH-flavin oxidoreductase: cloning, sequencing and overexpression of the gene and purification and characterization of the cloned enzyme
J. Bacteriol.
176
3552-3558
1994
Vibrio harveyi, Vibrio harveyi MAV / ATCC 33843
brenda
Mack, C.P.; Hultquist, D.E.; Shlafer, M.
Myocardial flavin reductase and riboflavin: a potential role in decreasing reoxygenation injury
Biochem. Biophys. Res. Commun.
212
35-40
1995
Oryctolagus cuniculus
brenda
Tanner, J.J.; Lei, B.; Tu, S.C.; Krause, K.L.
Flavin reductase P: structure of a dimeric enzyme that reduces flavin
Biochemistry
35
13531-13539
1996
Vibrio harveyi
brenda
Liu, M.; Lei, B.; Ding, Q.; Lee, J.C.; Tu, S.C.
Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium
Arch. Biochem. Biophys.
337
89-95
1997
Vibrio harveyi
brenda
Parry, R.J.; Li, W.
An NADPH:FAD oxidoreductase from the valanimycin producer, Streptomyces viridifaciens. Cloning analysis, and overexpression
J. Biol. Chem.
272
23303-23311
1997
Streptomyces viridifaciens
brenda
Zenno, S.; Kobori, T.; Tanokura, M.; Saigo, K.
Purification and characterization of NfrA1, a Bacillus subtilis nitro/flavin reductase capable of interacting with the bacterial luciferase
Biosci. Biotechnol. Biochem.
62
1978-1987
1998
Bacillus subtilis, Bacillus subtilis ISW 1214.
brenda
Wang, H.; Lei, B.; Tu, S.C.
Vibrio harveyi NADPH-FMN oxidoreductase Arg203 as a critical residue for NADPH recognition and binding
Biochemistry
39
7813-7819
2000
Vibrio harveyi
brenda
Matsubara, T.; Ohshiro, T.; Nishina, Y.; Izumi, Y.
Purification, characterization, and overexpression of flavin reductase involved in dibenzothiophene desulfurization by Rhodococcus erythropolis D-1
Appl. Environ. Microbiol.
67
1179-1184
2001
Rhodococcus erythropolis, Rhodococcus erythropolis D1
brenda
Gao, B.; Ellis, H.R.
Altered mechanism of the alkanesulfonate FMN reductase with the monooxygenase enzyme
Biochem. Biophys. Res. Commun.
331
1137-1145
2005
Escherichia coli
brenda
Lei, B.; Wang, H.; Yu, Y.; Tu, S.C.
Redox potential and equilibria in the reductive half-reaction of Vibrio harveyi NADPH-FMN oxidoreductase
Biochemistry
44
261-267
2005
Aliivibrio fischeri, Vibrio harveyi
brenda
Kwasnicka, D.A.; Krakowiak, A.; Thacker, C.; Brenner, C.; Vincent, S.R.
Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and Hint-related 7meGMP-directed hydrolase, DCS-1
J. Biol. Chem.
278
39051-39058
2003
Caenorhabditis elegans, Homo sapiens (Q9UHB4), Homo sapiens
brenda
Low, J.C.; Tu, S.C.
Energy transfer evidence for in vitro and in vivo complexes of Vibrio harveyi flavin reductase P and luciferase
Photochem. Photobiol.
77
446-452
2003
Vibrio harveyi
brenda
Gao, B.; Bertrand, A.; Boles, W.H.; Ellis, H.R.; Mallett, T.C.
Crystallization and preliminary X-ray crystallographic studies of the alkanesulfonate FMN reductase from Escherichia coli
Acta Crystallogr. Sect. F
F61
837-840
2005
Escherichia coli
brenda
Li, X.; Tu, S.C.
Activity coupling of Vibrio harveyi luciferase and flavin reductase (FRP): oxygen as a probe
Arch. Biochem. Biophys.
454
26-31
2006
Vibrio harveyi
brenda
Li, X.; Chow, D.C.; Tu, S.C.
Thermodynamic analysis of the binding of oxidized and reduced FMN cofactor to Vibrio harveyi NADPH-FMN oxidoreductase FRP apoenzyme
Biochemistry
45
14781-14787
2006
Vibrio harveyi
brenda
Deller, S.; Sollner, S.; Trenker-El-Toukhy, R.; Jelesarov, I.; Guebitz, G.M.; Macheroux, P.
Characterization of a thermostable NADPH:FMN oxidoreductase from the mesophilic bacterium Bacillus subtilis
Biochemistry
45
7083-7091
2006
Bacillus subtilis
brenda
Okai, M.; Kudo, N.; Lee, W.C.; Kamo, M.; Nagata, K.; Tanokura, M.
Crystal structures of the short-chain flavin reductase HpaC from Sulfolobus tokodaii strain 7 in its three states: NAD(P)(+)-free, NAD(+)-bound, and NADP(+)-bound
Biochemistry
45
5103-5110
2006
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
brenda
Liu, G.; Zhou, J.; Lv, H.; Xiang, X.; Wang, J.; Zhou, M.; Qv, Y.
Azoreductase from Rhodobacter sphaeroides AS1.1737 is a flavodoxin that also functions as nitroreductase and flavin mononucleotide reductase
Appl. Microbiol. Biotechnol.
76
1271-1279
2007
Rhodobacter sphaeroides, Rhodobacter sphaeroides AS1.1737
brenda
Jawanda, N.; Ebalunode, J.; Gribenko, A.; Briggs, J.; Lee, J.C.; Tu, S.C.
A single-residue mutation destabilizes Vibrio harveyi flavin reductase FRP dimer
Arch. Biochem. Biophys.
472
51-57
2008
Vibrio harveyi
brenda
Jawanda, N.; Ahmed, K.; Tu, S.C.
Vibrio harveyi flavin reductase-luciferase fusion protein mimics a single-component bifunctional monooxygenase
Biochemistry
47
368-377
2008
Vibrio harveyi
brenda
Tu, S.C.
Activity coupling and complex formation between bacterial luciferase and flavin reductases
Photochem. Photobiol. Sci.
7
183-188
2008
Aliivibrio fischeri, Vibrio harveyi
brenda
Vorontsov, I.I.; Minasov, G.; Brunzelle, J.S.; Shuvalova, L.; Kiryukhina, O.; Collart, F.R.; Anderson, W.F.
Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity
Protein Sci.
16
2483-2490
2007
Shigella flexneri
brenda
Campbell, Z.T.; Baldwin, T.O.
Fre Is the Major Flavin Reductase Supporting Bioluminescence from Vibrio harveyi Luciferase in Escherichia coli
J. Biol. Chem.
284
8322-8328
2009
Escherichia coli
brenda
Takahashi, S.; Furuya, T.; Ishii, Y.; Kino, K.; Kirimura, K.
Characterization of a flavin reductase from a thermophilic dibenzothiophene-desulfurizing bacterium, Bacillus subtilis WU-S2B
J. Biosci. Bioeng.
107
38-41
2009
Bacillus subtilis, Bacillus subtilis WU-S2B
brenda
Chikuba, K.; Yubisui, T.; Shirabe, K.; Takeshita, M.
Cloning and nucleotide sequence of a cDNA of the human erythrocyte NADPH-flavin reductase
Biochem. Biophys. Res. Commun.
198
1170-1176
1994
Homo sapiens (P30043), Homo sapiens
brenda
Yubisui, T.; Tamura, M.; Takeshita, M.
Characterization of a second form of NADPH-flavin reductase purified from human erythrocytes
Biochem. Int.
15
1-8
1987
Homo sapiens
brenda
Shalloe, F.; Elliott, G.; Ennis, O.; Mantle, T.J.
Evidence that biliverdin-IX beta reductase and flavin reductase are identical
Biochem. J.
316
385-387
1996
Bos taurus
brenda
Cunningham, O.; Gore, M.G.; Mantle, T.J.
Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXbeta reductase (BVR-B)
Biochem. J.
345
393-399
2000
Homo sapiens (P30043), Homo sapiens
brenda
Chung, H.W.; Tu, S.C.
Structure-function relationship of Vibrio harveyi NADPH-flavin oxidoreductase FRP: essential residues Lys167 and Arg15 for NADPH binding
Biochemistry
51
4880-4887
2012
Vibrio harveyi
brenda
Haynes, R.K.; Cheu, K.W.; Tang, M.M.; Chen, M.J.; Guo, Z.F.; Guo, Z.H.; Coghi, P.; Monti, D.
Reactions of antimalarial peroxides with each of leucomethylene blue and dihydroflavins: flavin reductase and the cofactor model exemplified
ChemMedChem
6
279-291
2011
Escherichia coli
brenda
Kozmin, S.G.; Wang, J.; Schaaper, R.M.
Role for CysJ flavin reductase in molybdenum cofactor-dependent resistance of Escherichia coli to 6-N-hydroxylaminopurine
J. Bacteriol.
192
2026-2033
2010
Escherichia coli
brenda
Zenno, S.; Kobori, T.; Tanokura, M.; Saigo, K.
Purification and characetrizatio of NfrA1, a Bacillus subtilis nitro/flavin reductase capable of interacting with the bacterial luciferase
Biosci. Biotechnol. Biochem.
62
1978-1987
1998
Bacillus subtilis, Bacillus subtilis ISW 1214
brenda
Man, Z.; Rao, Z.; Xu, M.; Guo, J.; Yang, T.; Zhang, X.; Xu, Z.
Improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply
Metab. Eng.
38
310-321
2016
Corynebacterium crenatum, Corynebacterium crenatum SYPA5-5
brenda
Leitsch, D.; Janssen, B.; Kolarich, D.; Johnson, P.; Duchene, M.
Trichomonas vaginalis flavin reductase 1 and its role in metronidazole resistance
Mol. Microbiol.
91
198-208
2014
Trichomonas vaginalis (A2GH85), Trichomonas vaginalis, Trichomonas vaginalis G3 (A2GH85)
brenda
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