The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.
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SYSTEMATIC NAME
IUBMB Comments
FADH2:NAD+ oxidoreductase
The enzyme from Burkholderia phenoliruptrix can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. Unlike EC 1.5.1.36, flavin reductase (NADH), the enzyme can not reduce riboflavin. The enzyme does not use NADPH as acceptor.
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
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
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)
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
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
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
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
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
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
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
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
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
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
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
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
the apparent molecular mass of the PrnD-PrnF complex appears to be approximately 120000 Da (gel filtration), confirming a 1:1 stoichiometry for binding of the two proteins, PrnD (86000 Da) and PrnF (39000 Da)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-form crystals of TftC, TftC-FAD complex and TftC-FAD-NADH complex are grown at 4°C using the hanging drop vapor diffusion method. Crystal structures of dimeric TftC is determined at 2.5 A resolution
to enable functional assessment of the two-component monooxygenase system in Baeyer-Villiger oxidations, recombinant plasmids expressing Fred (FMN reductase (NADH)) in tandem with the respective 2,5-diketocamphane- and 3,6-diketocamphane 1,2-monooxygenase-encoding genes in Escherichia coli are constructed
strain X1 Fre can effectively dehalogenate dihalophenols, which can be useful for the treatment of dihalophenols in wastewaters and remediation of DCP-contaminated environments
strain X1 Fre can effectively dehalogenate dihalophenols, which can be useful for the treatment of dihalophenols in wastewaters and remediation of DCP-contaminated environments
strain X1 Fre can effectively dehalogenate dihalophenols, which can be useful for the treatment of dihalophenols in wastewaters and remediation of DCP-contaminated environments
Characterization of SgcE6, the flavin reductase component supporting FAD-dependent halogenation and hydroxylation in the biosynthesis of the enediyne antitumor antibiotic C-1027
Chakraborty, S.; Ortiz-Maldonado, M.; Entsch, B.; Ballou, D.P.
Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from Pseudomonas aeruginosa: a system composed of a small flavin reductase and a large flavin-dependent oxygenase
Camphor pathway redux functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions