1.5.1.30: flavin reductase (NADPH)
This is an abbreviated version!
For detailed information about flavin reductase (NADPH), go to the full flat file.
Word Map on EC 1.5.1.30
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1.5.1.30
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monooxygenase
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mononucleotide
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harveyi
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flavin-dependent
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fmnh2
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dibenzothiophene
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fischeri
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desulfurization
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halogenases
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oxygen-insensitive
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nadh:flavin
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biodesulfurization
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nitroreductases
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leiognathi
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fadh2-dependent
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2-hydroxybiphenyl
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fmn-dependent
- 1.5.1.30
- monooxygenase
- mononucleotide
- harveyi
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flavin-dependent
- fmnh2
- dibenzothiophene
- fischeri
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desulfurization
- halogenases
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oxygen-insensitive
-
nadh:flavin
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biodesulfurization
- nitroreductases
- leiognathi
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fadh2-dependent
- 2-hydroxybiphenyl
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fmn-dependent
Reaction
Synonyms
alkanesulfonate FMN reductase, ArsH, azoreductase, AZRü, biliverdin IXbeta reductase, biliverdin reductase B, biliverdin reductase-B, Biliverdin-IX beta-reductase, BLVRB, CysJ, EC 1.6.8.2, FAD-dependent NADP-reductase, flavin oxidoreductase, flavin reductase, flavin reductase 1, flavin reductase Nr1, flavin reductase P, FLR, FR1, Frb, Frd188, frd2, fre, Fre oxidoreductase, Fre-1, FRG/FRaseI, FRGvf, FRP, FRPvh, GHBP, Green heme binding protein, HpaC, ipa-43d, LuxG, More, NAD(P)H-dependent H2O2-forming flavin reductase, NAD(P)H:flavin-oxidoreductase, NADPH-dependant FMN reductase, NADPH-dependent diaphorase, NADPH-flavin oxidoreductase, NADPH-flavin reductase, NADPH-FMN oxidoreductase, NADPH-FMN reductase, NADPH-nitrofurazone reductase, NADPH-specific flavin reductase, NADPH:FAD oxidoreductase, NADPH:flavin oxidoreductase, NADPH:FMN oxidoreductase, NfrA1, nitro/flavin reductase, non-luminescent-bacterial NfsA/Frp-type enzyme, SsuE, TVAG_517010
ECTree
1.5.1.30 flavin reductase (NADPH)Advanced search results
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results (Engineering
Engineering on EC 1.5.1.30 - flavin reductase (NADPH)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L114M/L165M
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mutant created to obtain selenomethionine-containing enzyme for crystallization. Activity of mutant is similar to wild-type, circular dichroism spectra identical to wiil-type
Q14R
mutation at active site arginine residue increases coenzyme affinity
Q14R/R78G
double mutation within the enzyme exhibits a binding affinity that is close to the average between these two individual mutations
R78A
mutation leads to both an increase in active site micro-millisecond motions and an increase in the microscopic rate constants of coenzyme binding
E99K
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the mutation destabilizes the dimer and has an enhanced subunit dissociation as evident from a 44fold higher Kd for the monomer-dimer equilibrium
K167A
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the mutant has apparently greatly increased Km and reduced kcat/Km for NADPH
R15A
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the mutant has apparently greatly increased Km and reduced kcat/Km for NADPH
R203A
additional information
R203A
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decrease of NADPH binding potential, critical role of Arg203 in the specific recognition and binding of NADPH
R203A
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site-directed mutagenesis, no reversibility of the reduction of FMN, the half-reaction
additional information
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improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd2, strain 5-5(frd2) and deletion strains 5-5DELTAfrd2 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutant 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd2) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview
additional information
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improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd2, strain 5-5(frd2) and deletion strains 5-5DELTAfrd2 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutant 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd2) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview
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additional information
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Fre oxidoreductase deletion strain shows 99% reduced bioluminescence in coupled assay with luciferase
additional information
generation of a WU2DELTAflaRkan null mutant strain
