1.5.1.36: flavin reductase (NADH)
This is an abbreviated version!
For detailed information about flavin reductase (NADH), go to the full flat file.
Word Map on EC 1.5.1.36
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1.5.1.36
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nadph:flavin
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fmnh2
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alkanesulfonate
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oxygen-insensitive
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beneckea
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desulfonation
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nitroreductases
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fmnh2-dependent
- 1.5.1.36
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nadph:flavin
- fmnh2
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alkanesulfonate
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oxygen-insensitive
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beneckea
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desulfonation
- nitroreductases
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fmnh2-dependent
Reaction
Synonyms
AbeF, BaiH, BorF, C1-HpaH, DszD, FAD reductase, FerA, flavin mononucleotide reductase, flavin reductase, flavin:NADH oxidoreductase, FMN reductase, Frd188, frd2, fre, HpaC, LJ0548, LJ0549, LJ_0548, LJ_0549, LuxG, More, NAD(P)H-dependent H2O2-forming flavin reductase, NAD(P)H-flavin oxidoreductase, NAD(P)H:flavin oxidoreductase, NAD(P)H:flavin-oxidoreductase, NADH-dependent flavin reductase, NADH-flavin oxidoreductase, NADH: flavin oxidoreductase, NADH: flavinoxidore ductase/NADH oxidase, NADH:flavin oxidoreductase, NADH:FMN oxidoreductase, nfr1, nfr2, NOX, Pden2689, SMOB-ADP1
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General Information
General Information on EC 1.5.1.36 - flavin reductase (NADH)
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evolution
malfunction
metabolism
physiological function
additional information
SMOB-ADP1 belongs to the flavin reductases of the HpaC-like subfamily. NAD(P)H:flavin oxidoreductase structure comparisons, overview
evolution
in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning
evolution
in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning
deletion of the encoding genes genes nfr1 and nfr2 in Lactobacillus johnsonii leads to a 40fold reduction of hydrogen peroxide formation. H2O2 production in this mutant can only be restored by in trans complementation of both genes
malfunction
inhibition of Nox causes a noticeable decrease in the microsclerotium yields. Silencing of Nox decreases the microsclerotium yield by 98.5%, H2O2 and virulence decrease it by 38% and 21.5%, respectively
malfunction
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inhibition of Nox causes a noticeable decrease in the microsclerotium yields. Silencing of Nox decreases the microsclerotium yield by 98.5%, H2O2 and virulence decrease it by 38% and 21.5%, respectively
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malfunction
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deletion of the encoding genes genes nfr1 and nfr2 in Lactobacillus johnsonii leads to a 40fold reduction of hydrogen peroxide formation. H2O2 production in this mutant can only be restored by in trans complementation of both genes
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in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate
metabolism
in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate
the 4-hydroxyphenylacetate 3-monooxygenase from Escherichia coli W is a two-component enzyme encoded by the hpaB and hpaC genes and catalyzes the initial reaction in the degradation of 4-hydroxyphenylacetate, i.e., the introduction of a second hydroxyl group into the benzene nucleus at a position ortho to the existing hydroxyl group, giving rise to 3,4-dihydroxyphenylacetate
physiological function
the conserved NADH-dependent flavin reductase is prominently involved in H2O2 production in Lactobacillus johnsonii, overview
physiological function
the enzyme Nox is required for microsclerotium differentiation through regulation of intracellular H2O2 concentration. Additionally Nox has a great impact on the virulence in Nomuraea rileyi in cabbage caterpillar
physiological function
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the enzyme Nox is required for microsclerotium differentiation through regulation of intracellular H2O2 concentration. Additionally Nox has a great impact on the virulence in Nomuraea rileyi in cabbage caterpillar
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physiological function
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the conserved NADH-dependent flavin reductase is prominently involved in H2O2 production in Lactobacillus johnsonii, overview
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stabilizing effect of another Paracoccus denitrificans protein, the NAD(P)H:acceptor oxidoreducase FerB, against spontaneous oxidation of the FerA-produced dihydroflavin. The turnover rate for NADH oxidation initiated by the addition of FMN is comparable to that for the native, untagged FerA, indicating that the His tag does not interfere with catalysis. Enzyme active ite structure analysis, overview
additional information
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stabilizing effect of another Paracoccus denitrificans protein, the NAD(P)H:acceptor oxidoreducase FerB, against spontaneous oxidation of the FerA-produced dihydroflavin. The turnover rate for NADH oxidation initiated by the addition of FMN is comparable to that for the native, untagged FerA, indicating that the His tag does not interfere with catalysis. Enzyme active ite structure analysis, overview
additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases
additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases
additional information
enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases
additional information
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His160 and Arg38 contribute to the catalytic activity and the pH dependence
additional information
His160 and Arg38 contribute to the catalytic activity and the pH dependence
additional information
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stabilizing effect of another Paracoccus denitrificans protein, the NAD(P)H:acceptor oxidoreducase FerB, against spontaneous oxidation of the FerA-produced dihydroflavin. The turnover rate for NADH oxidation initiated by the addition of FMN is comparable to that for the native, untagged FerA, indicating that the His tag does not interfere with catalysis. Enzyme active ite structure analysis, overview
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