The Enzyme Database

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Accepted name: FMN reductase (NADH)
Reaction: FMNH2 + NAD+ = FMN + NADH + H+
For diagram of FAD biosynthesis, click here
Other name(s): NADH-FMN reductase; NADH-dependent FMN reductase; NADH:FMN oxidoreductase; NADH:flavin oxidoreductase
Systematic name: FMNH2:NAD+ oxidoreductase
Comments: The enzyme often forms a two-component system with monooxygenases. Unlike EC, FMN reductase (NADPH), and EC, FMN reductase [NAD(P)H], this enzyme has a strong preference for NADH over NADPH, although some activity with the latter is observed [1,2]. While FMN is the preferred substrate, FAD can also be used with much lower activity [1,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Duane, W. and Hastings, J.W. Flavin mononucleotide reductase of luminous bacteria. Mol. Cell. Biochem. 6 (1975) 53–64. [PMID: 47604]
2.  Gerlo, E. and Charlier, J. Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi. Eur. J. Biochem. 57 (1975) 461–467. [DOI] [PMID: 1175652]
3.  Uetz, T., Schneider, R., Snozzi, M. and Egli, T. Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600. J. Bacteriol. 174 (1992) 1179–1188. [DOI] [PMID: 1735711]
4.  Izumoto, Y., Mori, T. and Yamamoto, K. Cloning and nucleotide sequence of the gene for NADH:FMN oxidoreductase from Vibrio harveyi. Biochim. Biophys. Acta 1185 (1994) 243–246. [DOI] [PMID: 8167139]
[EC created 2011]

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