1.5.1.39: FMN reductase [NAD(P)H]
This is an abbreviated version!
For detailed information about FMN reductase [NAD(P)H], go to the full flat file.
Reaction
Synonyms
ChuY, EC 1.5.1.29, EC 1.6.8.1, flavin mononucleotide reductase, FMN reductase, fre, FRG, H2O-forming FOR, LrFOR, NAD(P)H-flavin reductase, NAD(P)H:FMN-oxidoreductase, NADH: FMN oxidoreductase, NADPH-dependent FMN reductase, NfoR, non-specific NAD(P)H-FMN reductase, pden_5119, Red, SsuE, two-component FMN-dependent monooxygenase, water forming NADH: FMN oxidoreductase
ECTree
1.5.1.39 FMN reductase [NAD(P)H]Advanced search results
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results (Substrates Products
Substrates Products on EC 1.5.1.39 - FMN reductase [NAD(P)H]
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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
FMN + NADH + H+
FMNH2 + NAD+
reductive and oxidative half reactions, kinetics, overview
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r
FMN + NADH + H+
FMNH2 + NAD+
reductive and oxidative half reactions, kinetics, overview
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r
FMN + NADPH + H+
FMNH2 + NADP+
reductive and oxidative half reactions, kinetics, overview
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r
FMN + NADPH + H+
FMNH2 + NADP+
reductive and oxidative half reactions, kinetics, overview
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r
FMNH2 + NAD+
FMN + NADH + H+
the enzyme exhibits about the same reaction rates with NADH and NADPH
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?
FMNH2 + NAD+
FMN + NADH + H+
the enzyme exhibits about the same reaction rates with NADH and NADPH
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?
additional information
?
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FMN enzyme binding structure analysis using wild-type and mutant enzymes, overview
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additional information
?
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the purified recombinant LrFOR has both the NADPH and NADH oxidation activity. The optimum FMN concentration for the LrFOR is 0.015 mM. With increasing of FMN concentration from 0.001 to 0.015 mM, the relative activity of LrFOR is also increased from 42% to 100%. When the concentration of FMN is increased to 0.030 mM, LrFOR displays more than 90% of the optimal activity. And the activity retains more than 80% of the optimal value when the FMN concentration is 0.070 mM
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additional information
?
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Lacticaseibacillus rhamnosus ATCC 53103
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the purified recombinant LrFOR has both the NADPH and NADH oxidation activity. The optimum FMN concentration for the LrFOR is 0.015 mM. With increasing of FMN concentration from 0.001 to 0.015 mM, the relative activity of LrFOR is also increased from 42% to 100%. When the concentration of FMN is increased to 0.030 mM, LrFOR displays more than 90% of the optimal activity. And the activity retains more than 80% of the optimal value when the FMN concentration is 0.070 mM
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additional information
?
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the enzyme-FMN complex is a functional oxidase that conducts the reduction of oxygen by NADH. Hydrogen peroxide is identified as the main product. The binding affinity for FMN does not dramatically change with flavin reduction. Oxygen behaves as a true substrate interacting with the enzyme only after dissociation of the first product, NAD+. The enzyme exhibits weak activity with ferricyanide, ubiquinone-0, 1,4-naphthoquinone and nitrofurantoin, while almost no activity is detected with hydrogen peroxide or disulfidic Ellman's reagent. The enzyme is also active in reducing the nonfluorescent N-oxide resazurin to the fluorescent resorufin. The initial-rate kinetics of fluorescence increase measured at various concentrations of NADH, and resazurin obeye the ping-pong mechanism as is observed for oxygen. Oxygen act as a competitive inhibitor of the reduction of resazurin, suggesting that these two electron acceptors are competing for the reduced flavin. The catalytic cycle involves an obligatory release of the formed FMNH2 because its back oxidation to FMN cannot occur in the absence of oxygen
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additional information
?
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the enzyme-FMN complex is a functional oxidase that conducts the reduction of oxygen by NADH. Hydrogen peroxide is identified as the main product. The binding affinity for FMN does not dramatically change with flavin reduction. Oxygen behaves as a true substrate interacting with the enzyme only after dissociation of the first product, NAD+. The enzyme exhibits weak activity with ferricyanide, ubiquinone-0, 1,4-naphthoquinone and nitrofurantoin, while almost no activity is detected with hydrogen peroxide or disulfidic Ellman's reagent. The enzyme is also active in reducing the nonfluorescent N-oxide resazurin to the fluorescent resorufin. The initial-rate kinetics of fluorescence increase measured at various concentrations of NADH, and resazurin obeye the ping-pong mechanism as is observed for oxygen. Oxygen act as a competitive inhibitor of the reduction of resazurin, suggesting that these two electron acceptors are competing for the reduced flavin. The catalytic cycle involves an obligatory release of the formed FMNH2 because its back oxidation to FMN cannot occur in the absence of oxygen
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additional information
?
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the enzyme-FMN complex is a functional oxidase that conducts the reduction of oxygen by NADH. Hydrogen peroxide is identified as the main product. The binding affinity for FMN does not dramatically change with flavin reduction. Oxygen behaves as a true substrate interacting with the enzyme only after dissociation of the first product, NAD+. The enzyme exhibits weak activity with ferricyanide, ubiquinone-0, 1,4-naphthoquinone and nitrofurantoin, while almost no activity is detected with hydrogen peroxide or disulfidic Ellman's reagent. The enzyme is also active in reducing the nonfluorescent N-oxide resazurin to the fluorescent resorufin. The initial-rate kinetics of fluorescence increase measured at various concentrations of NADH, and resazurin obeye the ping-pong mechanism as is observed for oxygen. Oxygen act as a competitive inhibitor of the reduction of resazurin, suggesting that these two electron acceptors are competing for the reduced flavin. The catalytic cycle involves an obligatory release of the formed FMNH2 because its back oxidation to FMN cannot occur in the absence of oxygen
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additional information
?
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transient-state FMN reduction, overview. Both rapid NADPH binding and hydride transfer to FMN in NfoR. The low relative rate observed is likely a function of the limiting concentration of FMN present or the trapping of the enzyme in an inhibitory product complex (e.g. NfoR-FMNH2-NADPH) in which the release of FMNH2 and/or NADPH is slow. Reoxidation of flavins (FADH2) by chromate and copper
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