FMN reductase (NADH) (EC 1.5.1.42, NADH-FMN reductase) is an enzyme with systematic name FMNH2:NAD+ oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reaction
| FMN reductase (NADH) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.1.42 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- FMNH2 + NAD+ FMN + NADH + H+
The enzyme often forms a complex with monooxygenases.
References
edit- ^ Duane W, Hastings JW (January 1975). "Flavin mononucleotide reductase of luminous bacteria". Molecular and Cellular Biochemistry. 6 (1): 53–64. doi:10.1007/BF01731866. PMID 47604.
- ^ Gerlo E, Charlier J (September 1975). "Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi" (PDF). European Journal of Biochemistry. 57 (2): 461–7. doi:10.1111/j.1432-1033.1975.tb02321.x. PMID 1175652.
- ^ Uetz T, Schneider R, Snozzi M, Egli T (February 1992). "Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600". Journal of Bacteriology. 174 (4): 1179–88. doi:10.1128/jb.174.4.1179-1188.1992. PMC 206410. PMID 1735711.
- ^ Izumoto Y, Mori T, Yamamoto K (April 1994). "Cloning and nucleotide sequence of the gene for NADH:FMN oxidoreductase from Vibrio harveyi". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1185 (2): 243–6. doi:10.1016/0005-2728(94)90216-x. PMID 8167139.
External links
edit- FMN+reductase+(NADH) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
