EC 1.5.1.42 - FMN reductase (NADH)

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.5.1.42

Names

Accepted name:
FMN reductase (NADH)
Other names:
NADH-FMN reductase
NADH-dependent FMN reductase
NADH:FMN oxidoreductase
NADH:flavin oxidoreductase
Systematic name:
FMNH2:NAD+ oxidoreductase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (69) [show] [UniProt]

References

  1. Duane, W., Hastings, J. W.
    Flavin mononucleotide reductase of luminous bacteria.
    Mol. Cell. Biochem. 6 : 53-64 (1975). [PMID: 47604]
  2. Gerlo, E., Charlier, J.
    Identification of NADH-specific and NADPH-specific FMN reductases in Beneckea harveyi.
    Eur. J. Biochem. 57 : 461-467 (1975). [PMID: 1175652]
  3. Uetz, T., Schneider, R., Snozzi, M., Egli, T.
    Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600.
    J. Bacteriol. 174 : 1179-1188 (1992). [PMID: 1735711]
  4. Izumoto, Y., Mori, T., Yamamoto, K.
    Cloning and nucleotide sequence of the gene for NADH:FMN oxidoreductase from Vibrio harveyi.
    Biochim. Biophys. Acta 1185 : 243-246 (1994). [PMID: 8167139]

[EC 1.5.1.42 created 2011]