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Information on EC 1.5.1.38 - FMN reductase (NADPH)
for references in articles please use BRENDA:EC1.5.1.38
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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
1.5.1.38 FMN reductase (NADPH)
IUBMB Comments
The enzymes from bioluminescent bacteria contain FMN , while the enzyme from Escherichia coli does not . The enzyme often forms a two-component system with monooxygenases such as luciferase. Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor [1,2]. While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity [3,6,8].
The expected taxonomic range for this enzyme is: Bacteria, Archaea
showSynonyms
nadph:fmn reductase, nad(p)h:fmn reductase, nadph specific fmn reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BC_1619
EC 1.5.1.29
-
-
formerly, part transferred
-
EC 1.6.8.1
-
-
formerly, part transferred
-
flavin reductase P
FRP
NADPH specific FMN reductase
NADPH-flavin oxidoreductase
NADPH:FMN oxidoreductase
SsuE
ydgI
additional information
flavin reductase P
-
-
-
-
FRP
-
-
-
-
SsuE
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FMNH2 + NADP+ = FMN + NADPH + H+
-
-
-
-
FMNH2 + NADP+ = FMN + NADPH + H+
the enzyme exhibits double displacement or ping-pong kinetics
-
FMNH2 + NADP+ = FMN + NADPH + H+
the first step in catalysis, which is hydride transfer from C4 of NADPH to cofactor FMN, involves addition to the re face of the FMN, probably at the N5 position. The limited accessibility of the FMN binding pocket and the extensive FMN-protein hydrogen bond network are consistent with the observed ping-pong bisubstrate-biproduct reaction kinetics
FMNH2 + NADP+ = FMN + NADPH + H+
the enzyme exhibits double displacement or ping-pong kinetics
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
bacterial bioluminescence, two-component alkanesulfonate monooxygenase
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SYSTEMATIC NAME
IUBMB Comments
FMNH2:NADP+ oxidoreductase
The enzymes from bioluminescent bacteria contain FMN [4], while the enzyme from Escherichia coli does not [8]. The enzyme often forms a two-component system with monooxygenases such as luciferase. Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor [1,2]. While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity [3,6,8].
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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
2-thioFMN + NADPH + H+
2-thioFMNH2 + NADP+
-
Substrates: the holoenzyme reconstituted with 2-thioFMN is catalytically active in using either FMN or 2-thioFMN as a substrate
Products: -
Products: -
?
FMN + NADH + H+
FMNH2 + NAD+
Substrates: when NADH is the pyrimidinic substrate, a distinct activity maximum is obtained at an FMN concentration of 0.5 mM, whereas concentrations higher than 2.5 mM led to more than 60% decrease in specific activity
Products: -
Products: -
?
FAD + NADPH + H+
FADH2 + NADP+
Substrates: FMN is the preferred flavin substrate of SsuE but FAD and riboflavin are also reduced at significant rates, whereas lumiflavin is not
Products: -
Products: -
?
FAD + NADPH + H+
FADH2 + NADP+
-
Substrates: Vmax/KM for riboflavin is 6fold lower compared to Vmax/Km for FMN
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
Substrates: FMN is the preferred flavin substrate of SsuE but FAD and riboflavin are also reduced at significant rates, whereas lumiflavin is not. When NADPH is supplied as pyrimidinic substrate, maximal reductase activity is obtained with 2.5-10 mM FMN, while higher FMN concentration leads to 15% decrease in SsuE activity. When NADH is the pyrimidinic substrate, a distinct activity maximum is obtained at an FMN concentration of 0.5 mM, whereas concentrations higher than 2.5 mM led to more than 60% decrease in specific activity
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: results from single-wavelength analyses at 450 and 550 nm show that reduction of FMN occurs in three distinct phases. Following a possible rapid equilibrium binding of FMN and NADPH to SsuE (MC-1) that occurs before the first detectable step, an initial fast phase (241 s-1) corresponds to the interaction of NADPH with FMN (CT-1). The second phase is a slow conversion (11 s-1) to form a charge-transfer complex of reduced FMNH2 with NADP+ (CT-2), and represents electron transfer from the pyridine nucleotide to the flavin. The third step (19 s-1) is the decay of the charge-transfer complex to SsuE with bound products (MC-2) or product release from the CT-2 complex. Results from isotope studies with [(4R)-2H]NADPH demonstrates a rate-limiting step in electron transfer from NADPH to FMN
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
Substrates: approximately one FMN is bound per monomer
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: -
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: the affinity of the NADPH-specific reductase for NADPH is 1000 times greater than for NADH
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: the apoenzyme binds one FMN per enzyme monomer with a dissociation constant of 0.2 mM at 23°C. The reconstituted holoenzyme is catalytically as active as the native enzyme. FMN binding results in 87% and 92% of quenching of protein and flavin fluorescence, respectively, indicating a conformational difference between the apoprotein and the holoenzyme. Neither riboflavin nor FAD shows any appreciable binding to the cofactor site of the apoenzyme but both flavins are active substrates for the FMN-containing holoenzyme. The holoenzyme reconstituted with 2-thioFMN is catalytically active in using either FMN or 2-thioFMN as a substrate
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: the NADPH specific FMN reductase does not utilize NADH
Products: -
Products: -
?
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: the NADPH specific FMN reductase does not utilize NADH
Products: -
Products: -
?
FMNH2 + NADP+
FMN + NADPH + H+
Substrates: FMN is enzyme-bound
Products: -
Products: -
r
FMNH2 + NADP+
FMN + NADPH + H+
Substrates: FMN is enzyme-bound
Products: -
Products: -
r
riboflavin + NADPH + H+
reduced riboflavin + NADP+
Substrates: FMN is the preferred flavin substrate of SsuE but FAD and riboflavin are also reduced at significant rates, whereas lumiflavin is not
Products: -
Products: -
?
riboflavin + NADPH + H+
reduced riboflavin + NADP+
-
Substrates: Vmax/KM for riboflavin is 13fold lower compared to Vmax/Km for FMN
Products: -
Products: -
?
additional information
?
-
Substrates: the nitroreductase of Bacillus cereus strain ATCC 14579 encoded by gene BC_1619 also shows NADPH-dependent FMN reductase activity, and interacts with the prodrug 5-(1-aziridinyl)-2,4-dinitrobenzamide, i.e. CB1954, converting it to either the toxic 2'- or 4'-hydroxylamine metabolites with cofactor NAD(P)H, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the nitroreductase of Bacillus cereus strain ATCC 14579 encoded by gene BC_1619 also shows NADPH-dependent FMN reductase activity, and interacts with the prodrug 5-(1-aziridinyl)-2,4-dinitrobenzamide, i.e. CB1954, converting it to either the toxic 2'- or 4'-hydroxylamine metabolites with cofactor NAD(P)H, overview
Products: -
Products: -
?
additional information
?
-
Substrates: electron transfer to ferricyanide is performed with FMN-bound Y118A SsuE mutant varying concentrations of NADPH, and ferricyanide, the ferricyanide concentration is saturating to maintain pseudo-first-order kinetic conditions at varying NADPH concentrations
Products: -
Products: -
?
additional information
?
-
Substrates: FMN binds tightly in a deeply held site, which makes available a second binding site, in which either a second FMN or the nicotinamide of NADPH can bind. The FMNH2-bound structure shows subtle changes consistent with its binding being weaker than that of FMN
Products: -
Products: -
?
additional information
?
-
Substrates: flavin reductases of two-component systems must transfer reduced flavin successfully to the monooxygenase enzymes for the insertion of single oxygen atom(s) into their respective substrates. Protein-protein interactions between the FMN-bound Y118 SsuE variants and SsuD, overview. A competition assay is performed with SsuE and SsuD. The enzyme also has desulfonation activity
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme also exhibits appreciable activity with some artificial acceptors: menadione, 2,6-dichlorophenolindophenol, KFeCN6 or 5,5'-dithiobis(2-nitrobenzoic acid). Low activity with methylene blue as acceptor
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also exhibits appreciable activity with some artificial acceptors: menadione, 2,6-dichlorophenolindophenol, KFeCN6 or 5,5'-dithiobis(2-nitrobenzoic acid). Low activity with methylene blue as acceptor
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
FMN + NADPH + H+
FMNH2 + NADP+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-thio-FMN
-
binds to the cofactor site of the apoenzyme with an affinity similar to that for FMN binding. The holoenzyme reconstituted with 2-thioFMN is catalytically active in using either FMN or 2-thioFMN as a substrate
NADH
kcat/KM for NADPH is 335fold higher compared to kcat/KM for NADH
additional information
the enzyme does not contain any bound flavin cofactor
-
FMN
-
the apoenzyme binds one FMN per enzyme monomer with a dissociation constant of 0.2 mM at 23°C. The reconstituted holoenzyme is catalytically as active as the native enzyme. FMN binding results in 87% and 92% of quenching of protein and flavin fluorescence, respectively, indicating a conformational difference between the apoprotein and the holoenzyme. Neither riboflavin nor FAD shows any appreciable binding to the cofactor site of the apoenzyme but both flavins are active substrates for the FMN-containing holoenzyme
FMN
the enzyme is specific for FMN as cofactor. FMN is recognized and tightly bound by a network of 16 hydrogen bonds, while steric considerations prevent the binding of FAD. A flexible loop containing a Lys and an Arg could account for the NADPH specificity
NADPH
-
the affinity of the NADPH-specific reductase for NADPH is 1000 times greater than for NADH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
when NADPH is supplied as pyrimidinic substrate, maximal reductase activity is obtained with 2.5-10 mM FMN, while higher FMN concentration led to 15% decrease in SsuE activity. When NADH is the pyrimidinic substrate, a distinct activity maximum is obtained at an FMN concentration of 0.5 mM, whereas concentrations higher than 2.5 mM led to more than 60% decrease in specific activity
additional information
-
FMN at concentrations over 0.002 mM significantly inhibits the coupled reaction in both light intensity and quantum yield, and shows apparent noncompetitive and competitive inhibition patterns against NADPH and luciferase, respectively. No inhibition of the NADPH oxidation is detected under identical conditions
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
2-thioFMN
-
pH 7.0, 23°C, enzyme derivative reconstituted from apoenzyme and 2-thioFMN
0.008
FMN
-
pH 7.0, 23°C, single-enzyme spectrophotometric assay monitoring the NADPH oxidation
0.003
NADPH
-
pH 7.0, 23°C, enzyme derivative reconstituted from apoenzyme and 2-thioFMN
0.02
NADPH
-
pH 7.0, 23°C, single-enzyme spectrophotometric assay monitoring the NADPH oxidation
additional information
additional information
-
the kinetic mechanism of FRP is changed to a sequential pattern with a Km(FMN) of 0.003 mM and a Km(NADPH) of 0.02 mM in a luciferase-coupled assay measuring light emission
-
additional information
additional information
steady-state kinetic analysis of wild-type and mutant enzymes, kinetics of FMN binding, overview
-
additional information
additional information
steady-state Michaelis-Menten kinetics, and rapid-reaction kinetic analyses of Y118A, DELTAY118 SsuE, and wild-type SsuE, as well as stopped-flow kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
the enzyme exhibits a maximum activity at pH 5.5 which drops to a broad shoulder from pH 6.5 to pH 8.5 with an activity 75% that of maximum at pH 7.0. About 60% of maximal activity at pH 5.0, about 50% of maximal activity at pH 10.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
the Tyr insertional residue of SsuE makes specific contacts across the dimer interface that may assist in the altered mechanistic properties of this enzyme. The Y118F SsuE variant maintains the Pi-Pi stacking interactions at the tetramer interface and has kinetic parameters similar to those of wild-type SsuE. Substitution of the Pi-helical residue (Tyr118) to Ala or Ser transforms the enzymes into flavin-bound SsuE variants that can no longer support flavin reductase and desulfonation activities. These variants exist as dimers and can form protein-protein interactions with SsuD even though flavin transfer is not sustained. The DELRAY118 SsuE variant is flavin-free as purified and does not undergo the tetramer to dimer oligomeric shift with the addition of flavin. The absence of desulfonation activity can be attributed to the inability of DELTAY118 SsuE to promote flavin transfer and undergo the requisite oligomeric changes to support desulfonation. Results from these studies provide insights into the role of the SsuE Pi-helix in promoting flavin transfer and oligomeric changes that support protein-protein interactions with SsuD
metabolism
a general catalytic cycle is proposed for two-component reductases of the flavodoxin-like superfamily, by which the enzyme can potentially provide FMNH2 to its partner monooxygenase by different routes depending on the FMN concentration and the presence of a partner monooxygenase SsueD, overview
physiological function
additional information
evolution
enzyme SsuE is part of the flavodoxin-like superfamily. A Pi-helix present at the tetramer building interface of enzyme Ssue is unique to the reductases from two-component monooxygenase systems
evolution
the flavin reductase of the alkanesulfonate monooxygenase system (SsuE) contains a conserved Pi-helix located at the tetramer interface that originates from the insertion of Tyr118 into helix alpha4 of SsuE, the presence of Pi-helices provides an evolutionary gain of function. Residue Tyr118 residue generates the Pi-helix in SsuE
evolution
the SsuE FMN reductase of the alkanesulfonate monooxygenase system belongs to the NAD(P)H:FMN reductase family based on a conserved flavodoxin fold. The subgroup of enzymes in the NAD(P)H:FMN reductase family is comprised of flavin reductases from two-component monooxygenase systems. The diverging structural feature in these FMN reductases is a Pi-helix centrally located at the tetramer interface that is generated by the insertion of an amino acid in a conserved alpha4 helix
physiological function
-
FMN reductase (SsuE) catalyzes the reduction of FMN by NADPH, and the reduced flavin is transferred to the monooxygenase (SsuD)
physiological function
NADPH:FMN oxidoreductase is involved in bioluminescence by providing reduced FMN to luciferase
physiological function
SsuD is a monooxygenase that catalyzes the desulfonation of alkanesulfonates and requires reduced FMN, which is provided by the NAD(P)H:flavin oxidoreductase SsuE
physiological function
the Pi-helix enables SsuE to effectively utilize flavin as a substrate in the two-component monooxygenase system of SsueE with SsueD, overview
additional information
at least a dimeric association is required for the function of enzyme SsuE, FMN binding site structure, overview
additional information
enzyme structure analysis, structure-function relationship and substrate binding, overview
Show AA Sequence and Transmembrane Helices (4073 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
40900
dimeric SsueE in presence of flavin, analytical ultracentrifugation
73100
tetrameric SsuE enzyme in the absence of flavin, analytical ultracentrifugation
additional information
-
formation of a stable complex between the flavin mononucleotide (FMN) reductase (SsuE) and monooxygenase (SsuD) of the alkanesulfonate monooxygenase system. The stoichiometry for protein-protein interactions is proposed to involve a 1:1 monomeric association of SsuE with SsuD. Interactions between the two proteins do not lead to overall conformational changes in protein structure
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
4 * 21300, recombinant wild-type enzyme and mutants DELTAY188 and Y118F enzyme, SDS-PAGE
monomer
additional information
analytical ultracentrifugation studies of SsuE confirm a dimer-tetramer equilibrium exists in solution, with FMN binding favoring the dimer. The active site includes residues from both subunits
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in apoform, or complexed with FMN or FMNH2, hanging drop vapour diffusion method, mixing 0.004 ml of 10 mg/ml of protein in 10 mM HEPES, pH 7.0, with 0.002 ml of reservoir solution containing 7.5% w/v PEG 3350 and 0.1 M sodium citrate, at room temperature, for complexed protein, the crystals are soaked in an AML containing 1 mM FMN solution, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution
vapor-diffusion technique yields single crystals that grow as hexagonal rods and diffract to 2.9 A resolution using synchrotron X-ray radiation. The protein crystallizes in the primitive hexagonal space group P622. Substitution of two leucine residues (Leu114 and Leu165) to methionine is performed to obtain selenomethionine-containing SsuE for MAD phasing. The selenomethionine derivative of SsuE has been expressed and purified and crystals of the protein have been obtained with and without bound FMN
-
the 1.8 A crystal structure of flavin reductase P from Vibrio harVeyi is solved by multiple isomorphous replacement and reveals that the enzyme is a unique dimer of interlocking subunits, with 9352 A(2) of surface area buried in the dimer interface. Each subunit comprises two domains
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y118A
Y118F
site-directed mutagenesis, altered kinetics compared to wild-type.The mutant forms tetramers like the wild-type
Y118S
site-directed mutagenesis, inability of Y118S SsuE to support desulfonation in the coupled assay. The mutant forms dimers in contrast to the wild-type
K167A
-
the mutant has apparently greatly increased Km and severely reduced kcat/Km values for NADPH and leads to a slight increase in kcat/Km for NADH
R15A
-
the mutant has apparently greatly increased Km and severely reduced kcat/Km values for NADPH
additional information
generation of a Y118 deletion mutant, DELTAY118, and of point mutants Y118S and Y118F. The Tyr insertional residue of SsuE makes specific contacts across the dimer interface that may assist in the altered mechanistic properties of this enzyme. The Y118F SsuE variant maintains the Pi-Pi stacking interactions at the tetramer interface and has kinetic parameters similar to those of wild-type SsuE. Substitution of the Pi-helical residue (Tyr118) to Ala or Ser transforms the enzymes into flavin-bound SsuE variants that can no longer support flavin reductase and desulfonation activities. These variants exist as dimers and can form protein-protein interactions with SsuD even though flavin transfer is not sustained. The DELTAY118 SsuE variant is flavin-free as purified and does not undergo the tetramer to dimer oligomeric shift with the addition of flavin. The absence of desulfonation activity can be attributed to the inability of DELTAY118 SsuE to promote flavin transfer and undergo the requisite oligomeric changes to support desulfonation. Results from these studies provide insights into the role of the SsuE Pi-helix in promoting flavin transfer and oligomeric changes that support protein-protein interactions with SsuD. A 10fold lower binding affinity for flavin binding is observed with the DELTAY118 SsuE deletion variant than with wild-type SsuE. Although the DELTAY118 SsuE variant is unable to support NADPH oxidase activity, the 10fold decrease in flavin affinity would not account for the absence of activity because the flavin should still bind at the saturating concentrations of FMN used in the flavin reductase assays. Inability of Y118A, Y118S, and DELTAY118 SsuE to support desulfonation in the coupled assay
Y118A
site-directed mutagenesis, the SsuE variant converts the typically flavin-free enzyme to a flavin-bound form. The Y118A SsuE FMN cofactor is reduced with approximately 1 equiv of NADPH in anaerobic titration experiments, and the flavin remains bound following reduction. No measurable sulfite product is formed in a coupled assays with the Y118A SsuE variant and SsuD, demonstrating that flavin transfer is no longer supported
Y118A
site-directed mutagenesis, altered kinetics compared to wild-type, inability of Y118A SsuE to support desulfonation in the coupled assay. The mutant forms dimers in contrast to the wild-type
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT