1.5.1.37: FAD reductase (NADH)
This is an abbreviated version!
For detailed information about FAD reductase (NADH), go to the full flat file.
Word Map on EC 1.5.1.37
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1.5.1.37
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reductases
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enediyne
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two-component
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peptidyl
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protein-tethered
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chromophore
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pathway-specific
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burkholderia
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cepacia
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halogenase
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halogenation
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globisporus
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fadh2-dependent
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chloro
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4-monooxygenase
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chlorophenol
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2,4,5-trichlorophenol
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flavin-dependent
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fluorescens
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arylamine
- 1.5.1.37
- reductases
-
enediyne
-
two-component
-
peptidyl
-
protein-tethered
- chromophore
-
pathway-specific
-
burkholderia
- cepacia
- halogenase
-
halogenation
- globisporus
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fadh2-dependent
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chloro
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4-monooxygenase
- chlorophenol
- 2,4,5-trichlorophenol
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flavin-dependent
- fluorescens
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arylamine
Reaction
Synonyms
FAD:NADH reductase, flavin reductase, flavin:NADH reductase, fre, Fred, HpaC, NAD(P)H:FAD reductase, NADH-dependent FAD reductase, NADH-FAD reductase, NADH:FAD oxidoreductase, NADH:flavin adenine dinucleotide oxidoreductase, PrnF, SgcE6, TftC
ECTree
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General Information
General Information on EC 1.5.1.37 - FAD reductase (NADH)
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metabolism
physiological function
additional information
the enzyme is involved in the degradation of (-)-camphor
metabolism
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the enzyme is involved in the degradation of (-)-camphor
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free FADH2 is generated by NADH:FAD oxidoreductase (TftC), and FADH2-dependent monooxygenase (TftD) uses FADH2 to separately transform 2,4,5-trichlorophenol and 2,5-dichloro-p-hydroquinone
physiological function
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TftD supplies FADH2 to (FADH2)-utilizing monooxygenase TftD, that converts 2,4,5-trichlorophenol to 2,5-dichloro-p-quinol and then to 5-chlorohydroxyquinol. It also converts 2,4,6-trichlorophenol to 2,6-dichloro-p-quinol as the final product
physiological function
the enzyme can adequately supply reduced flavin under saturating substrate conditions to support catalysis of flavin-dependent halogenase SgcC3 and monooxygenase SgcC during biosynthesis of C-1027
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substitution of an NADH dehydrogenase (down-regulated) by an up-regulated NADH:FAD oxidoreductase and upregulation of an ATP synthase subunit, alongside the observed shifts in the TCA cycle, suggested that an oxygen-scavenging electron transport chain likely remains active during low redox conditions
additional information
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the structure and active site of Fre is constructed and analyzed via homologous modeling and molecular docking
additional information
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substitution of an NADH dehydrogenase (down-regulated) by an up-regulated NADH:FAD oxidoreductase and upregulation of an ATP synthase subunit, alongside the observed shifts in the TCA cycle, suggested that an oxygen-scavenging electron transport chain likely remains active during low redox conditions
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additional information
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the structure and active site of Fre is constructed and analyzed via homologous modeling and molecular docking
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additional information
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the structure and active site of Fre is constructed and analyzed via homologous modeling and molecular docking
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