Information on EC 1.5.1.30 - flavin reductase (NADPH):
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EC NUMBERCOMMENTARY
1.5.1.30-

RECOMMENDED NAMEGeneOntology No.
flavin reductase (NADPH)GO:0042602

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
show the reaction diagram		----
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
show the reaction diagram		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 10foldEscherichia coli-657786
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
show the reaction diagram		catalytic mechanismVibrio harveyi-660061
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
show the reaction diagram		FRP:luciferase coupled reaction can utilize reduced flavin by both free diffusion and direct transferVibrio harveyi-671610
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
show the reaction diagram		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 cofoactorsVibrio harveyi-672105
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
show the reaction diagram		bi-bi ternary mechanism, i.e. both FMN and NADPH must bind to the active site before catalysis can occurBacillus subtilis-672184
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
show the reaction diagram		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 transferSulfolobus tokodaii-678187
reduced riboflavin + NADP+ = riboflavin + NADPH + H+
show the reaction diagram		ping-pong mechanismAliivibrio fischeri, Vibrio harveyi-689388

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
oxidation----
redox reaction----
redox reactionAliivibrio fischeri, Vibrio harveyi--689388
reduction----

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
reduced-riboflavin:NADP+ oxidoreductaseThe enzyme reduces riboflavin, and, less efficiently, FMN and FAD. NADH is oxidized less efficiently than NADPH.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
alkanesulfonate FMN reductaseEscherichia coli--657786
ArsHShigella flexneri--689909
azoreductaseRhodobacter sphaeroides-flavodoxin that also functions as nitroreductase and flavin mononucleotide reductase684610
AZRüRhodobacter sphaeroides--684610
Biliverdin-IX beta-reductase----
flavin oxidoreductaseEscherichia coli--698992
flavin reductaseStreptomyces globisporus--698001
flavin reductaseEscherichia coli--698992
flavin reductaseBacillus subtilis--699057
flavin reductase Nr1Homo sapiensQ9UHB4-659261
flavin reductase PVibrio harveyi--392299, 660061
FLR----
FrbBacillus subtilis--699057
Fre oxidoreductaseEscherichia coli--698992
Fre-1Caenorhabditis elegansQ9U2Y8-659261
Fre-1Homo sapiensQ9UHB4-659261
FRG/FRaseIAliivibrio fischeri--392205
FRGvfAliivibrio fischeri--689388
FRPVibrio harveyi--658108, 660061, 684711, 685230
FRPAliivibrio fischeri--658108
FRPvhVibrio harveyi--689388
GHBP----
Green heme binding protein----
NADPH-dependant FMN reductaseShigella flexneri--689909
NADPH-dependent diaphorase----
NADPH-flavin reductase----
NADPH-flavin reductaseHomo sapiensP30043-714010
NADPH-FMN oxidoreductaseVibrio harveyi--658108
NADPH-FMN reductaseHomo sapiens--392188
NADPH-specific flavin reductaseVibrio harveyi--684711
NADPH:FAD oxidoreductaseStreptomyces viridifaciens--392301
NADPH:flavin oxidoreductaseAliivibrio fischeri--392205
NADPH:flavin oxidoreductaseEntamoeba histolytica--392296
NADPH:flavin oxidoreductaseVibrio harveyi--392297
NADPH:FMN oxidoreductaseVibrio harveyi--392299, 392300, 392303
SgcE6Streptomyces globisporus-HpaC-like subfamily of class 1 flavin reductases698001
SsuEEscherichia coli--657786
HpaCSulfolobus tokodaii--678187
additional informationVibrio harveyi-see also EC 1.5.1.29658108, 660061
additional informationAliivibrio fischeri-see also EC 1.5.1.29658108

CAS REGISTRY NUMBERCOMMENTARY
56626-29-0-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Aliivibrio fischeri-392205, 658108, 689388--Manually annotated by BRENDA team
Bacillus subtilisenzyme additionally has azoreductase activity672184--Manually annotated by BRENDA team
Bacillus subtilisISW 1214.392302--Manually annotated by BRENDA team
Bacillus subtilisstrain WU-S2B699057--Manually annotated by BRENDA team
Bacillus subtilis ISW 1214.ISW 1214.392302--Manually annotated by BRENDA team
Bacillus subtilis WU-S2Bstrain WU-S2B699057--Manually annotated by BRENDA team
Bos taurus-714076--Manually annotated by BRENDA team
Caenorhabditis elegansgene fre-1659261Q9U2Y8SwissProtManually annotated by BRENDA team
Entamoeba histolyticastrain NIH:200392296--Manually annotated by BRENDA team
Entamoeba histolytica NIH:200strain NIH:200392296--Manually annotated by BRENDA team
Escherichia coli-698992--Manually annotated by BRENDA team
Escherichia colienzyme SsuE is part of alkanesulfonate monooxygenase system, together with a monooxygenase enzyme SsuD657786, 671139--Manually annotated by BRENDA team
Haloarcula sp. D1D1392304--Manually annotated by BRENDA team
Homo sapiens-392188, 714074--Manually annotated by BRENDA team
Homo sapiens-714010P30043UniProtManually annotated by BRENDA team
Homo sapiensbifunctional enzymebiliverdin reductase/flavin reductase (NADPH)714077P30043UniProtManually annotated by BRENDA team
Homo sapiensgene fre-1659261Q9UHB4SwissProtManually annotated by BRENDA team
Oryctolagus cuniculusNew Zealand white rabbits, ca. 1.5 kg each392298--Manually annotated by BRENDA team
Rhodobacter sphaeroidesstrain AS1.1737684610--Manually annotated by BRENDA team
Rhodobacter sphaeroides AS1.1737strain AS1.1737684610--Manually annotated by BRENDA team
Rhodococcus erythropolisD1392304--Manually annotated by BRENDA team
Shigella flexneri2a strain 2457T689909--Manually annotated by BRENDA team
Streptomyces globisporus-698001--Manually annotated by BRENDA team
Streptomyces viridifaciens-392301--Manually annotated by BRENDA team
Sulfolobus tokodaiistain 7678187--Manually annotated by BRENDA team
Vibrio harveyi-392299, 392300, 392303, 658108, 660061, 671610, 672105, 684711, 685230, 689388--Manually annotated by BRENDA team
Vibrio harveyistrain MAV or B392.392297--Manually annotated by BRENDA team
Vibrio harveyi MAVstrain MAV or B392.392297--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
metabolismBacillus subtilis-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 activities699057
physiological functionEscherichia coli-provides reducing equivalents required to drive the luciferase genes in Escherichia coli but is not coupled to luciferase698992

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-dinitrobenzene + NADH + H+? + NAD+
show the reaction diagram		Bacillus subtilis-10.6% activity compared to FMN699057--?
1,4-benzoquinone + NADH + H+1,4-benzoquinol + NAD+
show the reaction diagram		Bacillus subtilis-18.6% activity compared to FMN699057--?
2,6-dichlorophenolindophenol + NADH + H+reduced 2,6-dichlorophenolindophenol + NAD+
show the reaction diagram		Bacillus subtilis-23.0% activity compared to FMN699057--?
3-nitrophenol + NADH + H+? + NAD+
show the reaction diagram		Bacillus subtilis-8.95% activity compared to FMN699057--?
4-nitroacetophenone + NADH + H+? + NAD+
show the reaction diagram		Bacillus subtilis-17.9% activity compared to FMN699057--?
4-nitroaniline + NADH + H+? + NAD+
show the reaction diagram		Bacillus subtilis-4.91% activity compared to FMN699057--?
4-nitrobenzoate + NADH + H+? + NAD+
show the reaction diagram		Bacillus subtilis-21.2% activity compared to FMN699057--?
4-nitrophenol + NADH + H+? + NAD+
show the reaction diagram		Bacillus subtilis-8.07% activity compared to FMN699057--?
4-nitrotoluene + NADH + H+? + NAD+
show the reaction diagram		Bacillus subtilis-8.83% activity compared to FMN699057--?
cytochrome c + NADH + H+reduced cytochrome c + NAD+
show the reaction diagram		Bacillus subtilis-8.48% activity compared to FMN699057--?
FAD + NADH + H+FADH2 + NAD+
show the reaction diagram		Streptomyces globisporus--698001--?
FAD + NADH + H+FADH2 + NAD+
show the reaction diagram		Bacillus subtilis-58.1% activity compared to FMN699057--?
FAD + NADPHFADH2 + NADP+
show the reaction diagram		Aliivibrio fischeri--392205--?
FAD + NADPHFADH2 + NADP+
show the reaction diagram		Entamoeba histolytica--392296--?
FAD + NADPHFADH2 + NADP+
show the reaction diagram		Streptomyces viridifaciens--392301--?
FAD + NADPH + H+FADH2 + NADP+
show the reaction diagram		Homo sapiensP30043-714077--?
FAD + NADPH + H+FADH2 + NADP+
show the reaction diagram		Homo sapiens-specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar714074--?
ferricyanide + NADH + H+ferrocyanide + NAD+
show the reaction diagram		Bacillus subtilis-15.4% activity compared to FMN699057--?
FMN + NAD(P)HFMNH2 + NAD(P)+
show the reaction diagram		Aliivibrio fischeri--689388--r
FMN + NADHFMNH2 + NAD+
show the reaction diagram		Rhodobacter sphaeroides--684610--?
FMN + NADHFMNH2 + NADP+
show the reaction diagram		Bacillus subtilis-preference for NADPH over NADH, rate of reduction is 80 times faster with NADPH672184--?
FMN + NADH + H+FMNH2 + NAD+
show the reaction diagram		Bacillus subtilis--699057--?
FMN + NADH + H+FMNH2 + NAD+
show the reaction diagram		Escherichia coli--698992--?
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Aliivibrio fischeri--392205--?
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Bacillus subtilis--392302--?
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Escherichia coli--657786--?
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Rhodobacter sphaeroides--684610--?
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Entamoeba histolytica--392296--?
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Vibrio harveyi--660061---
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Vibrio harveyi--392297, 392300, 392303, 684711, 685230--?
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Vibrio harveyi--689388--r
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Rhodococcus erythropolis--392304--?
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Shigella flexneri--689909--r
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Streptomyces viridifaciens--392301--?
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Bacillus subtilis-preference for NADPH over NADH, rate of reduction is 80 times faster with NADPH672184--?
FMN + NADPHFMNH2 + NADP+
show the reaction diagram		Vibrio harveyi-reaction may be coupled with luciferase for bioluminescence671610--?
FMN + NADPHFMNH2 + NADP+ + H+
show the reaction diagram		Escherichia coli--698992--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Escherichia coli--698992--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Homo sapiens--392188--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Streptomyces globisporus--698001--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Homo sapiensP30043-714077--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Bacillus subtilis-203% activity compared to NAD699057--?
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Homo sapiens-specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar714074--?
galactoflavin + NADPHreduced galactoflavin + NADP+
show the reaction diagram		Entamoeba histolytica--392296--?
lumiflavin + NADH + H+reduced lumiflavin + NAD+
show the reaction diagram		Bacillus subtilis-14.1% activity compared to FMN699057--?
menadione + NADH + H+menadiol + NAD+
show the reaction diagram		Bacillus subtilis-19.0% activity compared to FMN699057--?
methyl-4-nitrobenzoate + NADH + H+? + NAD+
show the reaction diagram		Bacillus subtilis-10.7% activity compared to FMN699057--?
nitrofurantoin + NADH + H+? + NAD+
show the reaction diagram		Bacillus subtilis-10.1% activity compared to FMN699057--?
nitrofurazone + NADH + H+reduced nitrofurazone + NAD+
show the reaction diagram		Bacillus subtilis-13.5% activity compared to FMN699057--?
nitrofurazone + NADPH + 4 H+5-(hydroxyamino)furan-2-carbaldehyde semicarbazone + NADP+ + H2O
show the reaction diagram		Bacillus subtilis--392302--?
oxidized 2,6-dichlorophenolindophenol + NADPH + H+reduced 2,6-dichlorophenolindophenol + NADP+
show the reaction diagram		Homo sapiens--714074--?
oxidized methylene blue + NADPH + H+reduced methylene blue + NADP+
show the reaction diagram		Homo sapiens--714074--?
oxidized riboflavin + NADPH + H+reduced riboflavin + NADP+
show the reaction diagram		Homo sapiensP30043-714077--?
oxidized riboflavin + NADPH + H+reduced riboflavin + NADP+
show the reaction diagram		Homo sapiens-specific activity for the reduction of oxidized riboflavin, FMN and FAD is similar714074--?
riboflavin + NAD(P)Hreduced riboflavin + NAD(P)+
show the reaction diagram		Aliivibrio fischeri--689388--r
riboflavin + NAD(P)Hreduced riboflavin + NADP+
show the reaction diagram		Aliivibrio fischeri-redox potential of the irreversible reductive half-reaction658108--?
riboflavin + NADH + H+reduced riboflavin + NAD+
show the reaction diagram		Bacillus subtilis-29.0% activity compared to FMN699057--?
riboflavin + NADPHreduced riboflavin + NADP+
show the reaction diagram		Aliivibrio fischeri--392205--?
riboflavin + NADPHreduced riboflavin + NADP+
show the reaction diagram		Entamoeba histolytica--392296--?
riboflavin + NADPHreduced riboflavin + NADP+
show the reaction diagram		Vibrio harveyi--392300, 660061--?
riboflavin + NADPHreduced riboflavin + NADP+
show the reaction diagram		Vibrio harveyi--689388--r
riboflavin + NADPHreduced riboflavin + NADP+
show the reaction diagram		Streptomyces viridifaciens--392301--?
riboflavin + NADPHreduced riboflavin + NADP+
show the reaction diagram		Vibrio harveyi-i.e. FMN660061i.e. FMNH2-?
riboflavin + NADPHreduced riboflavin + NADP+
show the reaction diagram		Vibrio harveyi-redox potential and equilibria in the reversible reductive half-reaction658108--?
riboflavin + NADPH + H+reduced riboflavin + NADP+
show the reaction diagram		Escherichia coli--698992--?
methylene blue + NADH + H+reduced methylene blue + NAD+
show the reaction diagram		Bacillus subtilis-29.0% activity compared to FMN699057--?
additional information?-Vibrio harveyi-enzyme transfers reduced riboflavin 5'-phosphate to luciferase by direct channeling in vitro and in vivo, formation of donor-acceptor enzyme complex660061---
additional information?-Bacillus subtilis-enzyme additionally has azoreductase activity cleaving the -N=N- bond in azo dyes672184---
additional information?-Shigella flexneri-no catalytic activity is detected with NADH689909---
additional information?-Rhodobacter sphaeroides-prefers NADPH over NADH684610---
additional information?-Bos taurus-bifunctional enzyme flavin reductase (NADPH)/biliverdin-IXbeta reductase714076---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
FAD + NADH + H+FADH2 + NAD+
show the reaction diagram		Streptomyces globisporus--698001--
FMN + NADH + H+FMNH2 + NAD+
show the reaction diagram		Bacillus subtilis--699057--
FMN + NADH + H+FMNH2 + NAD+
show the reaction diagram		Escherichia coli--698992--
FMN + NADPHFMNH2 + NADP+ + H+
show the reaction diagram		Escherichia coli--698992--
riboflavin + NADPHreduced riboflavin + NADP+
show the reaction diagram		Aliivibrio fischeri--392205--
riboflavin + NADPHreduced riboflavin + NADP+
show the reaction diagram		Entamoeba histolytica--392296--
riboflavin + NADPHreduced riboflavin + NADP+
show the reaction diagram		Vibrio harveyi--392300, 660061--
riboflavin + NADPHreduced riboflavin + NADP+
show the reaction diagram		Streptomyces viridifaciens--392301--
FMN + NADPH + H+FMNH2 + NADP+
show the reaction diagram		Bacillus subtilis-203% activity compared to NAD699057--
additional information?-Vibrio harveyi-enzyme transfers reduced riboflavin 5'-phosphate to luciferase by direct channeling in vitro and in vivo, formation of donor-acceptor enzyme complex660061--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
2-thio-FMNAliivibrio fischeri--392205 2D-image
2-thio-FMNVibrio harveyi--392300 2D-image
FADAliivibrio fischeri--392205 2D-image
FADStreptomyces viridifaciens--392301 2D-image
FMNAliivibrio fischeri--392205 2D-image
FMNVibrio harveyi-tightly bound392297 2D-image
FMNVibrio harveyi--392299, 392303, 671610, 685230 2D-image
FMNVibrio harveyi-no cofactors are FAD and riboflavin392300 2D-image
FMNBacillus subtilis--392302, 699057 2D-image
FMNEscherichia coli--657786 2D-image
FMNAliivibrio fischeri, Vibrio harveyi-1 FMN bound per subunit of the dimeric enzyme658108 2D-image
FMNBacillus subtilis-noncovalently bound672184 2D-image
FMNSulfolobus tokodaii-one molecule per monomer of enzyme. FMN is preferred over FAD678187 2D-image
FMNRhodobacter sphaeroides-the presence of exogenously added FMN is necessary for activity684610 2D-image
FMNVibrio harveyi-contains one bound FMN cofactor per subunit684711 2D-image
FMNAliivibrio fischeri, Vibrio harveyi-contains one FMN cofactor per monomer, the FMN cofactor of FRPVh can be replaced by 2-thioFMN to yield a catalytically active reconstituted reductase689388 2D-image
FMNShigella flexneri--689909 2D-image
NAD(P)HAliivibrio fischeri--658108, 689388 2D-image
NADHRhodococcus erythropolis-without any chromophore like flavin, NADPH is inert392304 2D-image
NADHBacillus subtilis--672184, 699057 2D-image
NADHRhodobacter sphaeroides-prefers NADPH over NADH684610 2D-image
NADHStreptomyces globisporus--698001 2D-image
NADP+Sulfolobus tokodaii--678187 2D-image
NADPHHomo sapiens-the FMN reductase activity is highly specific for NADPH, and the activity with NADH is 10% of that with NADPH392188 2D-image
NADPHEntamoeba histolytica-20fold selectivity over NADH392296 2D-image
NADPHBacillus subtilis--392302, 672184, 699057 2D-image
NADPHVibrio harveyi--392303, 658108, 660061, 671610, 684711, 685230, 689388 2D-image
NADPHEscherichia coli--657786 2D-image
NADPHCaenorhabditis elegansQ9U2Y8dependent on659261 2D-image
NADPHHomo sapiensQ9UHB4dependent on659261 2D-image
NADPHRhodobacter sphaeroides-preferred cofactor684610 2D-image
NADPHShigella flexneri--689909 2D-image
riboflavinAliivibrio fischeri--392205 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
CaCl2Bacillus subtilis-with 1 mM 84.5% activity699057
FeCl2Bacillus subtilis-with 1 mM 90.0% activity699057
MgCl2Bacillus subtilis-with 1 mM 92.6% activity699057
NiCl2Bacillus subtilis-with 1 mM 86.6% activity699057
ZnCl2Bacillus subtilis-with 1 mM 96.8% activity699057
MnCl2Bacillus subtilis-with 1 mM 97.0% activity699057
additional informationHomo sapiens-Fe2+, Fe3+, Mg2+, and Ca2+ do not affect the enzyme activity392188

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1,10-phenanthrolineHomo sapiens--392188 2D-image
2,3-diphosphoglycerateHomo sapiens--392188 2D-image
5,5'-dithiobis(2-nitrobenzoic acid)Bacillus subtilis-with 0.1 mM 28.8% activity699057 2D-image
7-hydroxycoumarinRhodococcus erythropolis--392304 2D-image
AcrinolHomo sapiens--392188 2D-image
Ag+Rhodococcus erythropolis--392304 2D-image
AgNO3Bacillus subtilis-with 1 mM 1.05% activity699057 2D-image
AmaranthShigella flexneri-the presence of 50 mM amaranth reduces the NADPH oxidation rate 2.6fold689909 2D-image
Bathocuproine sulfonateHomo sapiens--392188 2D-image
Cibacron MarineBacillus subtilis-azo dye, competitive to NADPH and FMN672184 2D-image
Cu2+Homo sapiens--392188 2D-image
Cu2+Rhodococcus erythropolis--392304 2D-image
CuCl2Bacillus subtilis-with 1 mM 11.2% activity699057 2D-image
Hg+Rhodococcus erythropolis--392304 2D-image
HgCl2Homo sapiens--392188 2D-image
HgCl2Bacillus subtilis-with 1 mM 0.77% activity699057 2D-image
lumichromeHomo sapiensP30043competitive inhibitor against FMN and a mixed inhibitor of NADPH714077 2D-image
N-ethylmaleimideBacillus subtilis-with 1 mM 16.3% activity699057 2D-image
NADP+Homo sapiens-0.1 mM, about 50% inhibition at no inhibition by NAD+ at pH 7.5, 12% inhibition at pH 4.8392188 2D-image
NADP+Escherichia coli--657786 2D-image
NADPHEscherichia coli--657786 2D-image
NEMRhodococcus erythropolis-when the enzyme is preincubated with NEM and NADH in the absence of FMN392304 2D-image
p-chloromercuribenzoic acidRhodococcus erythropolis--392304 2D-image
p-chloromercuribenzoic acidBacillus subtilis-with 1 mM 15.6% activity699057 2D-image
PCMBHomo sapiens--392188 2D-image
Ponceau BSShigella flexneri-the presence of 50 mM Ponceau BS reduces the NADPH oxidation rate 3.7fold689909 2D-image
proflavin hemisulfateHomo sapiens--392188-
SeO32-Homo sapiens--392188 2D-image
Zn2+Homo sapiens--392188 2D-image
mesobiliverdin XIIIaHomo sapiensP30043competitive kinetics with FMN and mixed inhibition kinetics with NADPH714077-
additional informationBacillus subtilis-with 1 mM ethylenediaminetetraacetic acid 99.8% activity, with 1 mM 2,2'-bipyridyl 81.8% activity699057-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
NADHEscherichia coli--698992 2D-image
NADHBacillus subtilis--699057 2D-image
NADPHEscherichia coli--698992 2D-image
NADPHBacillus subtilis-about double activity compared to NADH699057 2D-image
additional informationCaenorhabditis elegansQ9U2Y8enzyme coexpression with gene dcs-1 is induced by heat shock659261-
additional informationHomo sapiensQ9UHB4enzyme coexpression with gene dcs-1 is induced by heat shock659261-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.007-2-thioFMNVibrio harveyi-enzyme reconstituted from apoenzyme and 2-thioFMN392300 2D-image
0.0036-FADStreptomyces viridifaciens--392301 2D-image
0.01-FADEntamoeba histolytica--392296 2D-image
0.125-FADHomo sapiensP30043pH 7.5, 25°C714077 2D-image
1.6e-05-FMNEscherichia coli-25°C, single-enzyme assay657786 2D-image
0.00013-FMNEscherichia coli-25°C, enzyme in complex with monooxygenase SsuD, presence of octanesulfonate657786 2D-image
0.00013-FMNVibrio harveyi-presence of 1.05 mM O2671610 2D-image
0.0009-FMNEscherichia coli-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 luciferase698992 2D-image
0.002-FMNVibrio harveyi-mutant enzyme E99K, in 50 mM phosphate buffer, at pH 7.0, at 23°C684711 2D-image
0.0047-FMNBacillus subtilis--392302 2D-image
0.005-FMNVibrio harveyi--392300 2D-image
0.0058-FMNVibrio harveyi-flavin reductase P R203A392303 2D-image
0.006-FMNEntamoeba histolytica--392296 2D-image
0.0069-FMNVibrio harveyi-native flavin reductase P392303 2D-image
0.007-FMNVibrio harveyi--392297 2D-image
0.008-FMNVibrio harveyi-native enzyme, at 23°C in 50 mM phosphate buffer, pH 7.0685230 2D-image
0.0084-FMNStreptomyces viridifaciens--392301 2D-image
0.0108-FMNRhodococcus erythropolis--392304 2D-image
0.02-FMNBacillus subtilis-pH 7.5, 37°C672184 2D-image
0.021-FMNVibrio harveyi-recombinant fusion protein, pH 7.0, 23°C660061 2D-image
0.05-FMNHomo sapiens-pH and temperature not specified in the publication714074 2D-image
0.052-FMNHomo sapiensP30043pH 7.5, 25°C714077 2D-image
0.072-FMNVibrio harveyi-enzyme fused to luciferase, at 23°C in 50 mM phosphate buffer, pH 7.0685230 2D-image
14.2-FMNRhodobacter sphaeroides-in the presence of NADPH684610 2D-image
0.208-NADHRhodococcus erythropolis--392304 2D-image
0.5-NADHRhodobacter sphaeroides-in the presence of FMN684610 2D-image
0.65-NADHBacillus subtilis-pH 7.5, 37°C672184 2D-image
1.9e-05-NADPHVibrio harveyi-presence of 1.05 mM O2671610 2D-image
7e-05-NADPHVibrio harveyi-mutant enzyme E99K, in 50 mM phosphate buffer, at pH 7.0, at 23°C684711 2D-image
0.00085-NADPHBacillus subtilis-nitrofurazone as electron acceptor392302 2D-image
0.002-NADPHHomo sapiens-pH and temperature not specified in the publication714074 2D-image
0.003-NADPHVibrio harveyi-enzyme reconstituted from apoenzyme and 2-thioFMN392300 2D-image
0.0035-NADPHBacillus subtilis-FMN as electron accceptor392302 2D-image
0.0054-NADPHEscherichia coli-25°C, single-enzyme assay657786 2D-image
0.011-NADPHVibrio harveyi--392300 2D-image
0.02-NADPHVibrio harveyi--392297 2D-image
0.02-NADPHVibrio harveyi-native enzyme, at 23°C in 50 mM phosphate buffer, pH 7.0685230 2D-image
0.021-NADPHVibrio harveyi-native flavin reductase P392303 2D-image
0.032-NADPHStreptomyces viridifaciens-FAD as electron acceptor392301 2D-image
0.048-NADPHVibrio harveyi-recombinant fusion protein, pH 7.0, 23°C660061 2D-image
0.05-NADPHEntamoeba histolytica-at a saturating concentration of FMN392296 2D-image
0.31-NADPHVibrio harveyi-enzyme fused to luciferase, at 23°C in 50 mM phosphate buffer, pH 7.0685230 2D-image
0.55-NADPHBacillus subtilis-pH 7.5, 37°C672184 2D-image
0.71-NADPHVibrio harveyi-flavin reductase P R203A392303 2D-image
0.0163-nitrofurazoneBacillus subtilis--392302 2D-image
0.053-oxidized riboflavinHomo sapiensP30043pH 7.5, 25°C714077-
0.0013-riboflavinEscherichia coli-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 luciferase698992 2D-image
0.011-riboflavinStreptomyces viridifaciens--392301 2D-image
0.025-riboflavinVibrio harveyi--392300 2D-image
0.04-riboflavinEntamoeba histolytica--392296 2D-image
0.04-galactoflavinEntamoeba histolytica--392296 2D-image
additional information-additional informationAliivibrio fischeri, Vibrio harveyi-substrate and cofactor binding, reaction kinetics658108-
additional information-additional informationVibrio harveyi-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.671610-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.7-Cibacron MarineBacillus subtilis-pH 7.5, 37°C672184 2D-image
0.3-FADHomo sapiensP30043pH 7.5, 25°C714077 2D-image
51-FADStreptomyces viridifaciens--392301 2D-image
0.099-FMNHomo sapiensP30043pH 7.5, 25°C714077 2D-image
1.7-FMNEscherichia coli-25°C, enzyme in complex with monooxygenase SsuD, presence of octanesulfonate657786 2D-image
1.9-FMNEscherichia coli-25°C, single-enzyme assay657786 2D-image
11.7-FMNVibrio harveyi-enzyme fused to luciferase, at 23°C in 50 mM phosphate buffer, pH 7.0685230 2D-image
36-FMNVibrio harveyi--392297 2D-image
37.5-FMNVibrio harveyi-native enzyme, at 23°C in 50 mM phosphate buffer, pH 7.0685230 2D-image
45-FMNStreptomyces viridifaciens--392301 2D-image
54.38-FMNRhodobacter sphaeroides-in the presence of NADPH684610 2D-image
60-FMNBacillus subtilis-pH 7.5, 37°C672184 2D-image
53.8-NADPHVibrio harveyi-flavin reductase P R203A392303 2D-image
62-NADPHStreptomyces viridifaciens--392301 2D-image
69.5-NADPHVibrio harveyi-native flavin reductase P392303 2D-image
70-NADPHBacillus subtilis-pH 7.5, 37°C672184 2D-image
0.3-oxidized riboflavinHomo sapiensP30043pH 7.5, 25°C714077-
6.7-riboflavinStreptomyces viridifaciens--392301 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2.4-FADHomo sapiensP30043pH 7.5, 25°C71407710459
0.0012-FMNEscherichia coli-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 luciferase69899210560
1.9-FMNHomo sapiensP30043pH 7.5, 25°C71407710560
5.6-oxidized riboflavinHomo sapiensP30043pH 7.5, 25°C7140770
0.021-riboflavinEscherichia coli-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 luciferase69899216192

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.00338-7-hydroxycoumarinRhodococcus erythropolis--392304 2D-image
0.003-Cibacron MarineBacillus subtilis-substrate FMN, pH 7.5, 37°C672184 2D-image
0.015-Cibacron MarineBacillus subtilis-substrate NADPH, pH 7.5, 37°C672184 2D-image
0.076-lumichromeHomo sapiensP30043pH 7.5, 25°C714077 2D-image
0.00059-mesobiliverdin XIIIaHomo sapiensP30043pH 7.5, 25°C714077-
0.0139-NADP+Escherichia coli-25°C, single-enzyme assay657786 2D-image
0.0035-NADPHEscherichia coli-25°C, enzyme in complex with monooxygenase SsuD, presence of octanesulfonate657786 2D-image
0.0039-NADPHEscherichia coli-25°C, single-enzyme assay657786 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.37-Homo sapiens-pH 7.0, 25°C392188
22-Entamoeba histolytica--392296
42.1-Bacillus subtilis-FMN reduction with NADH, pH 6.0, 50°C699057
53-Bacillus subtilis--392302
85.5-Bacillus subtilis-FMN reduction with NADPH, pH 6.0, 50°C699057
88-Vibrio harveyi--392297
107-Streptomyces viridifaciens--392301
122-Rhodococcus erythropolis--392304
133-Rhodococcus erythropolis-flavin reductase from recombinant Escherichia coli392304
141-Streptomyces viridifaciens-without N-terminal His-tag392301
additional information-Streptomyces globisporus-10 mM Tris-HCl, pH 7.5, substrates: 160 microM NAD(P)H, 100 micro FAD or FMN698001

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
4.8-Homo sapiens--392188
4.9-Homo sapiens-citrate-phosphate buffer714074
5-Homo sapiensP30043sharp optimum, in citrate buffer714077
6-Rhodococcus erythropolis-enzyme assay392304
6-Bacillus subtilis--699057
7-Aliivibrio fischeri, Vibrio harveyi-assay at658108
7-Vibrio harveyi-assay at660061
7.5-Homo sapiensP30043assay at714077
8-Entamoeba histolytica-enzyme assay392296

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
410Bacillus subtilis-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 buffer699057
4.58Homo sapiens-pH 4.5: about 85% of maximal activity, pH 8.0: about 45% of maximal activity392188

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
23-Vibrio harveyi-enzyme assay392297
23-Bacillus subtilis-enzyme assay392302
23-Vibrio harveyi-assay at660061
25-Streptomyces viridifaciens-enzyme assay392301
25-Homo sapiensP30043assay at714077
35-Rhodococcus erythropolis-enzyme assay392304
50-Bacillus subtilis--699057

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2055Bacillus subtilis-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°C699057

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
6.1-Homo sapiens--714074
8.1-Homo sapiens--392188

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
cardiac muscleOryctolagus cuniculus--392298Manually annotated by BRENDA team
erythrocyteHomo sapiens--392188, 714010, 714074Manually annotated by BRENDA team
erythrocyteBos taurus--714076Manually annotated by BRENDA team
heartOryctolagus cuniculus-whole hearts392298Manually annotated by BRENDA team
HEK cellHomo sapiensQ9UHB4-659261Manually annotated by BRENDA team
kidneyOryctolagus cuniculus--392298Manually annotated by BRENDA team
kidney cell lineHomo sapiensQ9UHB4COS cell659261Manually annotated by BRENDA team
liverOryctolagus cuniculus--392298Manually annotated by BRENDA team
myocyteOryctolagus cuniculus--392298Manually annotated by BRENDA team
lungOryctolagus cuniculus--392298Manually annotated by BRENDA team
additional informationCaenorhabditis elegansQ9U2Y8genes fre-1 and dcs-1 are coordinately expressed through worm development659261Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
nucleusHomo sapiensQ9UHB4perinuclear5634659261Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
21270-Streptomyces viridifaciens-calculated from sequence of cloned DNA392301
22000-Homo sapiens-gel filtration392188
23000-Streptomyces viridifaciens-SDS-PAGE392301
26000-Escherichia coli-SDS-PAGE698992
26320-Vibrio harveyi-calculated from sequence of cloned DNA392297
28320-Bacillus subtilis-calculated from sequence of cDNA392302
3000038000Vibrio harveyi-gel filtration392300
33000-Vibrio harveyi-gel filtration392297
36000-Streptomyces viridifaciens-gel filtration392301
40000-Entamoeba histolytica-gel filtration392296
40000-Bacillus subtilis-SDS-PAGE699057
49200-Aliivibrio fischeri-X-ray crystallography689388
52600-Vibrio harveyi-X-ray crystallography689388
76000-Bacillus subtilis-gel filtration672184
86000-Rhodococcus erythropolis-gel filtration392304
113600-Shigella flexneri-dynamic light scattering689909

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Homo sapiens-x * 21500, SDS-PAGE392188
?Bacillus subtilis-x * 28000, SDS-PAGE392302
?Vibrio harveyi-x * 53783, recombinant fusion protein, sequence calculation660061
?Homo sapiens-x * 22000, SDS-PAGE714074
dimerVibrio harveyi-dimerization of native enzyme and apoenzyme, equilibrium ultracentrifugation392300
dimerAliivibrio fischeri, Vibrio harveyi--658108
dimerVibrio harveyi-2 * 26300684711
dimerVibrio harveyi-2 * 26300, gel filtration685230
homodimerVibrio harveyi-FMN binding pocket, crystallization, X-ray392299
homodimerStreptomyces viridifaciens--392301
homodimerAliivibrio fischeri-2 * 24600, X-ray crystallography689388
homodimerVibrio harveyi-2 * 26300, X-ray crystallography689388
homodimerBacillus subtilis-2 * 20000699057
homotetramerRhodococcus erythropolis-4 * 22000, SDS-PAGE392304
monomerEntamoeba histolytica-1 * 38000-40000, SDS-PAGE392296
monomerVibrio harveyi-1 * 28000, wild type and cloned, SDS-PAGE392297
monomerAliivibrio fischeri, Vibrio harveyi-in solution FRPVh undergoes a monomer-dimer equilibrium689388
monomerEscherichia coli-1 * 26000698992
tetramerBacillus subtilis-4 * 21000, SDS-PAGE672184
tetramerShigella flexneri-4 * 28400, dynamic light scattering, ArsH in solution at room temperature does exist predominantly in the tetrameric form; dimer of dimer, X-ray crystallography689909

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
selenomethionine derivative of mutant L114M/L165MEscherichia coli-671139
sitting drop vapour diffusion method, using 0.2 M calcium chloride and 20% (w/v) polyethylene glycol 3350Shigella flexneri-689909
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 transferSulfolobus tokodaii-678187

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
212Bacillus subtilis-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 buffer699057
68.5Rhodococcus erythropolis--392304

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
2070Bacillus subtilis-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°C699057
86.5-Bacillus subtilis-melting point of protein672184
100-Homo sapiens-boiling of the enzyme leads to complete loss of the FMN reductase activity392188

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
freezing and thawing causes no appreciable loss of the enzyme activityHomo sapiens-392188
stable at temperatures below 50°CRhodococcus erythropolis-392304

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
4°C, the purified enzyme is stable atHomo sapiens-392188

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
recombinant enzyme from Escherichia coli to homogeneityAliivibrio fischeri-658108
-Bacillus subtilis-392302
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 bufferBacillus subtilis-699057
bifunctional enzyme flavin reductase (NADPH)/biliverdin-IXbeta reductaseBos taurus-714076
-Entamoeba histolytica-392296
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 7.0Escherichia coli-698992
-Homo sapiens-392188, 714074
-Rhodococcus erythropolis-392304
-Shigella flexneri-689909
-Streptomyces globisporus-698001
-Streptomyces viridifaciens-392301
FMN-agarose chromatography as a key stepVibrio harveyi-392297
preparation of apoenzymeVibrio harveyi-392300
recombinant enzyme from Escherichia coli strain BL21(DE3) to over 90% purity, recombinant fusion protein from Escherichia coli strain JM109 to over 80% purityVibrio harveyi-660061
recombinant wild-type and mutant enzyme from Escherichia coli to homogeneityVibrio harveyi-658108
the flavin reductase-luciferase fusion protein is purified using DEAE-cellulose DE-52 column chromatography, DEAE-Sepharose column chromatography, and Superdex 200 gel filtrationVibrio harveyi-685230
ultracentrifugation, G-25 gel filtration, DEAE-Sepharose column chromatography, and Sephadex G25 gel filtrationVibrio harveyi-684711

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression of wild-type enzyme in Escherichia coliAliivibrio fischeri-658108
expressed in Escherichia coliBacillus subtilis-392302
frb gene inserted into plasmid pET21-a, introduced into Escherichia coli BL21 (DE3), cultivated at 30°CBacillus subtilis-699057
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-1Caenorhabditis elegansQ9U2Y8659261
PCR-amplification, expression in Escherichia coli Bl21 (deltaDE3)Escherichia coli-698992
-Homo sapiensP30043714010
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-1Homo sapiensQ9UHB4659261
expressed in Escherichia coliRhodobacter sphaeroides-684610
-Rhodococcus erythropolis-392304
-Shigella flexneri-689909
overexpression of SgcE6 gene in Escherichia coliStreptomyces globisporus-698001
expressed in Escherichia coliStreptomyces viridifaciens-392301
expressed in Escherichia coliVibrio harveyi-392297, 392299, 392303
expressed in Escherichia coli BL21 cellsVibrio harveyi-684711, 685230
expression of wild-type enzyme and mutant R203A in Escherichia coliVibrio harveyi-658108
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 T203YVibrio harveyi-660061

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
E99KVibrio harveyi-the mutation destabilizes the dimer and has an enhanced subunit dissociation as evident from a 44fold higher Kd for the monomer-dimer equilibrium684711
R203AVibrio harveyi-decrease of NADPH binding potential, critical role of Arg203 in the specific recognition and binding of NADPH392303
R203AVibrio harveyi-site-directed mutagenesis, no reversibility of the reduction of FMN, the half-reaction658108
L114M/L165MEscherichia coli-mutant created to obtain selenomethionine-containing enzyme for crystallization. Activity of mutant is similar to wild-type, circular dichroism spectra identical to wiil-type671139
additional informationEscherichia coli-Fre oxidoreductase deletion strain shows 99% reduced bioluminescence in coupled assay with luciferase698992

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.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 holoenzymeVibrio harveyi-684711

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
medicineStreptomyces globisporus-enzyme provides reduced flavin for flavin-dependent halogenase SgcC3 and monooxygenase SgcC, that install chloro- and hydroxy-substituents to the Streptomyces globisporus antitumor antibiotic C-1027 enediyne698001

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
Amyotrophic Lateral SclerosisPartial loss of NADPH-diaphorase/nitric oxide synthase-complex in amyotrophic lateral sclerosis and human type-II myofiber atrophy. PubMed
LeukemiaPurification of an NADPH-dependent diaphorase from membrane of DMSO-induced differentiated human promyelocytic leukemia HL-60 cells. PubMed
MethemoglobinemiaFlavin reductase: sequence of cDNA from bovine liver and tissue distribution. PubMed
Whooping Cough[Cloning and analysis of genes encoding 2-naphthoate monooxygenase and NADH:flavin oxidoreductase] PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
392188Yubisui, T.; Matsuki, T.; Takeshita, M.; Yoneyama, Y.Characterization of the purified NADPH-flavin reductase of human erythrocytesJ. Biochem.85719-7281979Homo sapiens PubMed
392205Tang, 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 IArch. Biochem. Biophys.392110-1162001Aliivibrio fischeri PubMed
392296Lo, H.S.; Reeves, R.E.Purification and properties of NADPH: flavin oxidoreductase from Entamoeba histolyticaMol. Biochem. Parasitol.223-301980Entamoeba histolytica PubMed
392297Lei, 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 enzymeJ. Bacteriol.1763552-35581994Vibrio harveyi PubMed
392298Mack, C.P.; Hultquist, D.E.; Shlafer, M.Myocardial flavin reductase and riboflavin: a potential role in decreasing reoxygenation injuryBiochem. Biophys. Res. Commun.21235-401995Oryctolagus cuniculus PubMed
392299Tanner, J.J.; Lei, B.; Tu, S.C.; Krause, K.L.Flavin reductase P: structure of a dimeric enzyme that reduces flavinBiochemistry3513531-135391996Vibrio harveyi PubMed
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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.1.30)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)