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Information on EC 1.5.1.30 - flavin reductase (NADPH)
for references in articles please use BRENDA:EC1.5.1.30
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.1 With NAD+ or NADP+ as acceptor
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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 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
-
fmn-dependent
showSynonyms
flavin reductase, blvrb, nadph-dependent diaphorase, flavin oxidoreductase, biliverdin reductase b, nadph-flavin reductase, nadph:fmn oxidoreductase, flavin reductase p, nadph:flavin oxidoreductase, nfra1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
azoreductase
AZRü
biliverdin reductase B
Biliverdin-IX beta-reductase
-
-
-
-
BLVRB
EC 1.6.8.2
-
-
formerly
-
flavin reductase
flavin reductase 1
FLR
-
-
-
-
FR1
Frb
Frd188
frd2
fre
Fre-1
FRP
GHBP
-
-
-
-
Green heme binding protein
-
-
-
-
HpaC
ipa-43d
NAD(P)H-dependent H2O2-forming flavin reductase
NAD(P)H:flavin-oxidoreductase
NADPH-dependent diaphorase
-
-
-
-
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
Cereibacter sphaeroides AS1.1737
-
flavodoxin that also functions as nitroreductase and flavin mononucleotide reductase
-
NADPH-flavin 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
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,3-dinitrobenzene + NADH + H+
? + NAD+
-
Substrates: 10.6% activity compared to FMN
Products: -
Products: -
?
1,4-benzoquinone + NADH + H+
1,4-benzoquinol + NAD+
-
Substrates: 18.6% activity compared to FMN
Products: -
Products: -
?
3-nitrophenol + NADH + H+
? + NAD+
-
Substrates: 8.95% activity compared to FMN
Products: -
Products: -
?
4-nitroacetophenone + NADH + H+
? + NAD+
-
Substrates: 17.9% activity compared to FMN
Products: -
Products: -
?
4-nitroaniline + NADH + H+
? + NAD+
-
Substrates: 4.91% activity compared to FMN
Products: -
Products: -
?
4-nitrobenzoate + NADH + H+
? + NAD+
-
Substrates: 21.2% activity compared to FMN
Products: -
Products: -
?
4-nitrophenol + NADH + H+
? + NAD+
-
Substrates: 8.07% activity compared to FMN
Products: -
Products: -
?
4-nitrotoluene + NADH + H+
? + NAD+
-
Substrates: 8.83% activity compared to FMN
Products: -
Products: -
?
FAD + NADH + H+
FADH2 + NAD+
-
Substrates: 58.1% activity compared to FMN
Products: -
Products: -
?
FMN + NADH
FMNH2 + NADP+
-
Substrates: preference for NADPH over NADH, rate of reduction is 80 times faster with NADPH
Products: -
Products: -
?
lumiflavin + NADH + H+
reduced lumiflavin + NAD+
-
Substrates: 14.1% activity compared to FMN
Products: -
Products: -
?
menadione + NADH + H+
menadiol + NAD+
-
Substrates: 19.0% activity compared to FMN
Products: -
Products: -
?
methyl-4-nitrobenzoate + NADH + H+
? + NAD+
-
Substrates: 10.7% activity compared to FMN
Products: -
Products: -
?
methylene blue + NADH + H+
reduced methylene blue + NAD+
-
Substrates: 29.0% activity compared to FMN
Products: -
Products: -
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
nitrofurantoin + NADH + H+
? + NAD+
-
Substrates: 10.1% activity compared to FMN
Products: -
Products: -
?
nitrofurazone + NADH + H+
reduced nitrofurazone + NAD+
-
Substrates: 13.5% activity compared to FMN
Products: -
Products: -
?
nitrofurazone + NADPH + 4 H+
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+
-
Substrates: -
Products: -
Products: -
?
oxidized methylene blue + NADPH + H+
reduced methylene blue + NADP+
-
Substrates: -
Products: -
Products: -
?
riboflavin + NAD(P)H
reduced riboflavin + NAD(P)+
-
Substrates: -
Products: -
Products: -
r
riboflavin + NAD(P)H
reduced riboflavin + NADP+
-
Substrates: redox potential of the irreversible reductive half-reaction
Products: -
Products: -
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
-
Substrates: 29.0% activity compared to FMN
Products: -
Products: -
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
Substrates: 15.4% activity compared to FMN
Products: -
Products: -
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
Substrates: 15.4% activity compared to FMN
Products: -
Products: -
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
Substrates: 8.48% activity compared to FMN
Products: -
Products: -
?
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
Substrates: 8.48% activity compared to FMN
Products: -
Products: -
?
FAD + NADPH + H+
FADH2 + NADP+
-
Substrates: specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
Products: -
Products: -
?
FAD + NADPH + H+
FADH2 + NADP+
Substrates: the enzyme (BLVRB) binds its coenzyme NADPH 500fold more tightly than its substrate FAD
Products: -
Products: -
?
FAD + NADPH + H+
FADH2 + NADP+
Substrates: -
Products: -
Products: -
r
FAD + NADPH + H+
reduced FAD + NADP+
-
Substrates: -
Products: -
Products: -
?
FMN + NADPH
FMNH2 + NADP+
-
Substrates: preference for NADPH over NADH, rate of reduction is 80 times faster with NADPH
Products: -
Products: -
?
FMN + NADPH
FMNH2 + NADP+
-
Substrates: -
Products: -
Products: -
?
FMN + NADPH
FMNH2 + NADP+
-
Substrates: reaction may be coupled with luciferase for bioluminescence
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: 203% activity compared to NAD+
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: 203% activity compared to NAD+
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
Products: -
Products: -
?
FMN + NADPH + H+
reduced FMN + NADP+
-
Substrates: -
Products: -
Products: -
?
galactoflavin + NADPH
reduced galactoflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
galactoflavin + NADPH
reduced galactoflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
lumiflavin + NADPH + H+
reduced lumiflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
lumiflavin + NADPH + H+
reduced lumiflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
Substrates: 23.0% activity compared to FMN
Products: -
Products: -
?
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
-
Substrates: 23.0% activity compared to FMN
Products: -
Products: -
?
nitrofurazone + NADPH + 4 H+
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
nitrofurazone + NADPH + 4 H+
5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
-
Substrates: -
Products: -
Products: -
?
oxidized riboflavin + NADPH + H+
reduced riboflavin + NADP+
Substrates: -
Products: -
Products: -
?
oxidized riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
Substrates: specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar
Products: -
Products: -
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
Substrates: i.e. FMN
Products: i.e. FMNH2
Products: i.e. FMNH2
?
riboflavin + NADPH
reduced riboflavin + NADP+
-
Substrates: redox potential and equilibria in the reversible reductive half-reaction
Products: -
Products: -
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
Substrates: -
Products: -
Products: -
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
Substrates: -
Products: -
Products: -
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
Substrates: -
Products: -
Products: -
?
riboflavin-5-phosphate + NADH + H+
reduced FMN + NAD+
-
Substrates: -
Products: -
Products: -
r
riboflavin-5-phosphate + NADH + H+
reduced FMN + NAD+
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: enzyme additionally has azoreductase activity cleaving the -N=N- bond in azo dyes
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional enzyme flavin reductase (NADPH)/biliverdin-IXbeta reductase
Products: -
Products: -
?
additional information
?
-
-
Substrates: prefers NADPH over NADH
Products: -
Products: -
?
additional information
?
-
Cereibacter sphaeroides AS1.1737
-
Substrates: prefers NADPH over NADH
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is also active with FMN and NADH, cf. EC 1.5.1.36
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is also active with FMN and NADH, cf. EC 1.5.1.36
Products: -
Products: -
?
additional information
?
-
-
Substrates: no catalytic activity is detected with NADH
Products: -
Products: -
?
additional information
?
-
Substrates: significant reduction of NADP+ by rFlaR refolded in the presence Fe2+. Fe2+ is the electron donor in the rFlaR-NADP+ reductase activity
Products: -
Products: -
-
additional information
?
-
Substrates: FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction
Products: -
Products: -
?
additional information
?
-
Substrates: FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme transfers reduced riboflavin 5'-phosphate to luciferase by direct channeling in vitro and in vivo, formation of donor-acceptor enzyme complex
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FAD + NADPH + H+
FADH2 + NADP+
Substrates: -
Products: -
Products: -
r
FAD + NADPH + H+
reduced FAD + NADP+
-
Substrates: -
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: 203% activity compared to NAD+
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: 203% activity compared to NAD+
Products: -
Products: -
?
FMN + NADPH + H+
reduced FMN + NADP+
-
Substrates: -
Products: -
Products: -
?
FMNH2 + NADP+
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