FMN reductase
| FMN reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.1.29 | ||||||||
| CAS no. | 64295-83-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an FMN reductase (EC 1.5.1.29) is an enzyme that catalyzes the chemical reaction
- FMNH2 + NAD(P)+ 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
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- Fisher J, Spencer R, Walsh C (1976). "Enzyme-catalyzed redox reactions with the flavin analogues 5-deazariboflavin, 5-deazariboflavin 5'-phosphate, and 5-deazariboflavin 5'-diphosphate, 5' leads to 5'-adenosine ester". Biochemistry. 15 (5): 1054–64. doi:10.1021/bi00650a016. PMID 3207.
- Tu SC, Becvar JE, Hastings JW (1979). "Kinetic studies on the mechanism of bacterial NAD(P)H:flavin oxidoreductase". Arch. Biochem. Biophys. 193 (1): 110–6. doi:10.1016/0003-9861(79)90013-4. PMID 222213.
- 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 (1): 89–95. doi:10.1006/abbi.1996.9746. PMID 8990272.
- Lei B, Tu SC (1998). "Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase". Biochemistry. 37 (41): 14623–9. doi:10.1021/bi981841+. 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 (1): 110–6. doi:10.1006/abbi.2001.2396. PMID 11469801.
- Ingelman M, Ramaswamy S, Niviere V, Fontecave M, Eklund H (1999). "Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli". Biochemistry. 38 (22): 7040–9. doi:10.1021/bi982849m. PMID 10353815.
- Eichhorn E, van der Ploeg JR, Leisinger T (1999). "Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli". J. Biol. Chem. 274 (38): 26639–46. doi:10.1074/jbc.274.38.26639. PMID 10480865.
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