| EC |
1.5.1.42 |
| Accepted name: |
FMN reductase (NADH) |
| Reaction: |
FMNH2 + NAD+ = FMN + NADH + H+ |
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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 1.5.1.38, FMN reductase (NADPH), and EC 1.5.1.39, 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 |
| References: |
| 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] |
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| [EC 1.5.1.42 created 2011] |
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