FMN reductase

In enzymology, a FMN reductase (EC 1.5.1.29) is an enzyme that catalyzes the chemical reaction

FMNH₂ + NAD(P)+ $\rightleftharpoons$ FMN + NAD(P)H + H⁺

The 3 substrates of this enzyme are FMNH2, NAD⁺, and NADP⁺, whereas its 4 products are FMN, NADH, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is FMNH2:NAD(P)+ oxidoreductase. Other names in common use include NAD(P)H-FMN reductase, NAD(P)H-dependent FMN reductase, NAD(P)H:FMN oxidoreductase, NAD(P)H:flavin oxidoreductase, NAD(P)H2 dehydrogenase (FMN), NAD(P)H2:FMN oxidoreductase, SsuE, riboflavin mononucleotide reductase, flavine mononucleotide reductase, riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide, (phosphate)) reductase, flavin mononucleotide reductase, and riboflavine mononucleotide reductase.

References

• Duane W, Hastings JW (1975). "Flavin mononucleotide reductase of luminous bacteria". Mol. Cell. Biochem. 6: 53–64. PMID 47604.
• Fisher J, Spencer R, Walsh C (1976). "Enzyme-catalyzed redox reactions with the flavin analogues 5-deazariboflavin, 5-deazariboflavin 5'-phosphte, and 5-deazariboflavin 5'-diphosphate, 5' leads to 5'-adenosine ester". Biochemistry. 15: 1054–64. PMID 3207.{{cite journal}}: CS1 maint: multiple names: authors list (link)
• Tu SC, Becvar JE, Hastings JW (1979). "Kinetic studies on the mechanism of bacterial NAD(P)H:flavin oxidoreductase". Arch. Biochem. Biophys. 193: 110–6. PMID 222213.{{cite journal}}: CS1 maint: multiple names: authors list (link)
• Liu M, Lei B, Ding Q, Lee JC, Tu SC (1997). "Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium". Arch. Biochem. Biophys. 337: 89–95. PMID 8990272.{{cite journal}}: CS1 maint: multiple names: authors list (link)
• Lei B, Tu SC (1998). "Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase". Biochemistry. 37: 14623–9. PMID 9772191.
• Tang CK, Jeffers CE, Nichols JC, Tu SC (2001). "Flavin specificity and subunit interaction of Vibrio fischeri general NAD(P)H-flavin oxidoreductase FRG/FRase I". Arch. Biochem. Biophys. 392: 110–6. PMID 11469801.{{cite journal}}: CS1 maint: multiple names: authors list (link)
• Ingelman M, Ramaswamy S, Niviere V, Fontecave M, Eklund H (1999). "Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli". Biochemistry. 38: 7040–9. PMID 10353815.{{cite journal}}: CS1 maint: multiple names: authors list (link)
• Eichhorn E, van der Ploeg JR, Leisinger T (1999). "Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli". J. Biol. Chem. 274: 26639–46. PMID 10480865.{{cite journal}}: CS1 maint: multiple names: authors list (link)

External links

The CAS registry number for this enzyme class is Template:CAS registry.