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
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halogenation
- globisporus
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fadh2-dependent
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chloro
-
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
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1.5.1.37 FAD reductase (NADH)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.5.1.37 - FAD reductase (NADH)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
lumiflavin + NADH + H+
reduced lumiflavin + NAD+
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6% of the activity with FAD
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-
?
riboflavin + NADH + H+
reduced riboflavin + NAD+
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9% of the activity with FAD
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-
?
FAD + NADH + H+
FADH2 + NAD+
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FAD is a better substrate than FMN. The enzyme does not use NADPH or riboflavin as substrate
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-
?
FAD + NADH + H+
FADH2 + NAD+
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the reductase catalyzes the reduction of FAD by NADH and releases the FADH- product into solution, but unlike the reductase from Actinetobacter baumannii, this catalysis is not influenced by p-hydroxyphenylacetate
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-
?
FAD + NADH + H+
FADH2 + NAD+
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involved in pyrrolnitrin biosynthesis. PrnF is the flavin:NADH reductase component of the two-component arylamine oxygenase system in Pseudomonas fluorescens Pf-5. PrnF reduces FAD to FADH2, which is then directly transferred to PrnD, where it is used by PrnD to catalyze the oxygenation of aminopyrrolnitrin. The PrnD oxygenase component requires a direct interaction with the PrnF reductase component to oxygenate arylamine
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-
?
FAD + NADH + H+
FADH2 + NAD+
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no activity with NADPH. PrnF reduces FAD to FADH2, which is then directly transferred to aminopyrrolnitrin oxygenase (PrnD), where it is used by PrnD to catalyze the oxygenation of aminopyrrolnitrin. The PrnD oxygenase component requires a direct interaction with the PrnF reductase component to oxygenate arylamine. Other flavin reductases present in the host cell would not supplant the role of PrnF. The turnover rate of PrnD in the presence of PrnF is almost two times higher than that in the presence of the Escherichia coli flavin SsuE reductase (EC 1.5.1.29)
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-
?
FAD + NADH + H+
FADH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
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-
?
FAD + NADH + H+
FADH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
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-
?
FAD + NADH + H+
FADH2 + NAD+
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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-
?
FAD + NADH + H+
FADH2 + NAD+
strictly NADH- and FAD-specific enzyme: No activity with NADPH or FMN
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-
?
FMN + NADH + H+
FMNH2 + NAD+
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FAD is a better substrate than FMN. The enzyme does not use NADPH or riboflavin as substrate
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-
?
FMN + NADH + H+
FMNH2 + NAD+
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HpaC can reduce either FAD or FMN
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-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
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-
?
FMN + NADH + H+
FMNH2 + NAD+
FMN and FAD are both substrates for the reductase. FMN is the favored substrate with a 2fold-higher rate constant and affinity that is about 5 times higher compared to that of FAD. With regard to electron donors, only NADH is effective whereas NADPH at a similar concentration acts as a very poor cosubstrate
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?
additional information
?
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Fre can effectively dehalogenate dihalophenols. Degradation of dichlorophenol (DCP) structural analogues by recombinant 2,4,6-trichlorophenol monooxygenase (TcpA) with NAD(P)H:FAD reductase (Fre), substrate specificities with 2,3-dichlorophenol (2,3-DCP), 2,4-dichlorophenol (2,4-DCP), 2,5-dichlorophenol (2,5-DCP), 2,6-dichlorophenol (2,6-DCP), 3,4-dichlorophenol (3,4 DCP), and 3,5-dichlorophenol (3,5-DCP), overview
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-
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additional information
?
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Fre can effectively dehalogenate dihalophenols. Degradation of dichlorophenol (DCP) structural analogues by recombinant 2,4,6-trichlorophenol monooxygenase (TcpA) with NAD(P)H:FAD reductase (Fre), substrate specificities with 2,3-dichlorophenol (2,3-DCP), 2,4-dichlorophenol (2,4-DCP), 2,5-dichlorophenol (2,5-DCP), 2,6-dichlorophenol (2,6-DCP), 3,4-dichlorophenol (3,4 DCP), and 3,5-dichlorophenol (3,5-DCP), overview
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-
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additional information
?
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Fre can effectively dehalogenate dihalophenols. Degradation of dichlorophenol (DCP) structural analogues by recombinant 2,4,6-trichlorophenol monooxygenase (TcpA) with NAD(P)H:FAD reductase (Fre), substrate specificities with 2,3-dichlorophenol (2,3-DCP), 2,4-dichlorophenol (2,4-DCP), 2,5-dichlorophenol (2,5-DCP), 2,6-dichlorophenol (2,6-DCP), 3,4-dichlorophenol (3,4 DCP), and 3,5-dichlorophenol (3,5-DCP), overview
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additional information
?
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methylene blue and ferricyanide are less than 5% as effective as FAD
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?
