EC 1.6.5.9 - NADH:ubiquinone reductase (non-electrogenic)

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IntEnz Enzyme Nomenclature
EC 1.6.5.9

Names

Accepted name:
NADH:ubiquinone reductase (non-electrogenic)
Other names:
ubiquinone reductase [ambiguous]
coenzyme Q reductase [ambiguous]
dihydronicotinamide adenine dinucleotide-coenzyme Q reductase [ambiguous]
DPNH-coenzyme Q reductase [ambiguous]
DPNH-ubiquinone reductase [ambiguous]
NADH-coenzyme Q oxidoreductase [ambiguous]
NADH-coenzyme Q reductase [ambiguous]
NADH-CoQ oxidoreductase [ambiguous]
NADH-CoQ reductase [ambiguous]
NADH-ubiquinone reductase [ambiguous]
NADH-ubiquinone oxidoreductase [ambiguous]
reduced nicotinamide adenine dinucleotide-coenzyme Q reductase [ambiguous]
NADH-Q6 oxidoreductase [ambiguous]
electron transfer complex I [ambiguous]
NADH2 dehydrogenase (ubiquinone) [ambiguous]
Systematic name:
NADH:quinone oxidoreductase

Reaction

Cofactor

Comments:

A flavoprotein (FAD or FMN). Occurs in mitochondria of yeast and plants, and in aerobic bacteria. Has low activity with NADPH. Unlike EC 7.1.1.2, NADH:ubiquinone reductase (H+-translocating), this enzyme does not pump proteons of sodium ions across the membrane. It is also not sensitive to rotenone.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (37) [show] [UniProt]

References

  1. Møller, I.M, and Palmer, J.M.
    Direct evidence for the presence of a rotenone-resistant NADH dehydrogenase on the inner surface of plant mitochondria.
    Physiol. Plant. 54 : 267-274 (1982).
  2. de Vries, S., Grivell, L. A.
    Purification and characterization of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria of Saccharomyces cerevisiae.
    Eur. J. Biochem. 176 : 377-384 (1988). [PMID: 3138118]
  3. Kerscher, S. J., Okun, J. G., Brandt, U.
    A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica.
    J. Cell. Sci. 112 : 2347-2354 (1999). [PMID: 10381390]
  4. Rasmusson, A. G., Soole, K. L., Elthon, T. E.
    Alternative NAD(P)H dehydrogenases of plant mitochondria.
    Annu. Rev. Plant. Biol. 55 : 23-39 (2004). [PMID: 15725055]
  5. Bergsma, J., Strijker, R., Alkema, J. Y., Seijen, H. G., Konings, W. N.
    NADH dehydrogenase and NADH oxidation in membrane vesicle from Bacillus subtilis.
    Eur. J. Biochem. 120 : 599-606 (1981). [PMID: 6800784]
  6. Melo, A. M., Bandeiras, T. M., Teixeira, M.
    New insights into type II NAD(P)H:quinone oxidoreductases.
    Microbiol. Mol. Biol. Rev. 68 : 603-616 (2004). [PMID: 15590775]

[EC 1.6.5.9 created 2011 (EC 1.6.5.11 created 1972 as EC 1.6.99.5, transferred 2015 to EC 1.6.5.11, incorporated 2019), modified 2019]