1.5.1.30: flavin reductase (NADPH)
This is an abbreviated version!
For detailed information about flavin reductase (NADPH), go to the full flat file.
Word Map on EC 1.5.1.30
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1.5.1.30
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monooxygenase
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mononucleotide
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harveyi
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flavin-dependent
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fmnh2
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dibenzothiophene
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fischeri
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desulfurization
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halogenases
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oxygen-insensitive
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nadh:flavin
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biodesulfurization
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nitroreductases
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leiognathi
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fadh2-dependent
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2-hydroxybiphenyl
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fmn-dependent
- 1.5.1.30
- monooxygenase
- mononucleotide
- harveyi
-
flavin-dependent
- fmnh2
- dibenzothiophene
- fischeri
-
desulfurization
- halogenases
-
oxygen-insensitive
-
nadh:flavin
-
biodesulfurization
- nitroreductases
- leiognathi
-
fadh2-dependent
- 2-hydroxybiphenyl
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fmn-dependent
Reaction
Synonyms
alkanesulfonate FMN reductase, ArsH, azoreductase, AZRü, biliverdin IXbeta reductase, biliverdin reductase B, biliverdin reductase-B, Biliverdin-IX beta-reductase, BLVRB, CysJ, EC 1.6.8.2, FAD-dependent NADP-reductase, flavin oxidoreductase, flavin reductase, flavin reductase 1, flavin reductase Nr1, flavin reductase P, FLR, FR1, Frb, Frd188, frd2, fre, Fre oxidoreductase, Fre-1, FRG/FRaseI, FRGvf, FRP, FRPvh, GHBP, Green heme binding protein, HpaC, ipa-43d, LuxG, More, NAD(P)H-dependent H2O2-forming flavin reductase, NAD(P)H:flavin-oxidoreductase, NADPH-dependant FMN reductase, NADPH-dependent diaphorase, NADPH-flavin oxidoreductase, NADPH-flavin reductase, NADPH-FMN oxidoreductase, NADPH-FMN reductase, NADPH-nitrofurazone reductase, NADPH-specific flavin reductase, NADPH:FAD oxidoreductase, NADPH:flavin oxidoreductase, NADPH:FMN oxidoreductase, NfrA1, nitro/flavin reductase, non-luminescent-bacterial NfsA/Frp-type enzyme, SsuE, TVAG_517010
ECTree
1.5.1.30 flavin reductase (NADPH)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.5.1.30 - flavin reductase (NADPH)
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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
-
-
?
FAD + NADPH + H+
FADH2 + NADP+
the enzyme (BLVRB) binds its coenzyme NADPH 500fold more tightly than its substrate FAD
-
-
?
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
?
-
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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
?
-
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bifunctional enzyme flavin reductase (NADPH)/biliverdin-IXbeta reductase
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-
?
additional information
?
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the enzyme is also active with FMN and NADH, cf. EC 1.5.1.36
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-
?
additional information
?
-
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the enzyme is also active with FMN and NADH, cf. EC 1.5.1.36
-
-
?
additional information
?
-
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no catalytic activity is detected with NADH
-
-
?
additional information
?
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significant reduction of NADP+ by rFlaR refolded in the presence Fe2+. Fe2+ is the electron donor in the rFlaR-NADP+ reductase activity
-
-
-
additional information
?
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FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction
-
-
?
additional information
?
-
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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
-
-
?
