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Literature summary for 1.6.5.9 extracted from

  • Velazquez, I.; Pardo, J.P.
    Kinetic characterization of the rotenone-insensitive internal NADH:ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae (2001), Arch. Biochem. Biophys., 389, 7-14.
    View publication on PubMed

General Stability

General Stability Organism
the enzyme is stable at low protein concentrations and in the presence of both substrates Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
2,6-dichlorophenolindophenol substrate inhibition Saccharomyces cerevisiae
AMP dead end reversible inhibitor, competitive inhibitor of NADH and uncompetitive inhibitor of 2,6-dichlorophenolindophenol Saccharomyces cerevisiae
flavone partial inhibitor Saccharomyces cerevisiae
additional information not inhibited by rotenone, NAD+ does not inhibit the activity of the enzyme, even at concentrations as high as 10 mM Saccharomyces cerevisiae
NADH substrate inhibition Saccharomyces cerevisiae
reduced 2,6-dichlorophenolindophenol product inhibition Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0062
-
2,6-dichlorophenolindophenol pH 7.0, 25°C Saccharomyces cerevisiae
0.0094
-
NADH pH 7.0, 25°C Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Saccharomyces cerevisiae 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53000
-
-
Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NADH + H+ + ubiquinone Saccharomyces cerevisiae
-
NAD+ + ubiquinol
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
DEAE Bio-gel column chromatography and Blue Sepharose CL-6B column chromatography, column chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the yeast enzyme is a two-electron reaction enzyme Saccharomyces cerevisiae ?
-
?
NADH + H+ + 2,6-dichlorophenolindophenol
-
Saccharomyces cerevisiae NAD+ + reduced 2,6-dichlorophenolindophenol
-
?
NADH + H+ + ubiquinone
-
Saccharomyces cerevisiae NAD+ + ubiquinol
-
?

Synonyms

Synonyms Comment Organism
Internal NADH dehydrogenase
-
Saccharomyces cerevisiae
NADH: ubiquinone oxidoreductase
-
Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
Saccharomyces cerevisiae

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.5 8 the free enzyme and the binary complex E-NADH are highly stable in the pH range from 5.5 to 8.0, maintaining the initial activity after 10 min incubation. Maximal stability is observed at pH 5.0 and 6.5 with no loss in activity. The enzyme is highly unstable above and below this pH range Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
FAD the mature enzyme contains FAD as prosthetic group Saccharomyces cerevisiae
additional information the mature enzyme contains no iron-sulfur clusters Saccharomyces cerevisiae
NADH
-
Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0054
-
flavone hyperbolic uncompetitive inhibition of NADH, pH 7.0, 25°C Saccharomyces cerevisiae
0.0071
-
flavone hyperbolic noncompetitive inhibition of 2,6-dichlorophenolindophenol, pH 7.0, 25°C Saccharomyces cerevisiae
0.0141
-
reduced 2,6-dichlorophenolindophenol pH 7.0, 25°C Saccharomyces cerevisiae
0.0525
-
NADH pH 7.0, 25°C Saccharomyces cerevisiae
0.1152
-
2,6-dichlorophenolindophenol pH 7.0, 25°C Saccharomyces cerevisiae
5.5
-
AMP linear competitive inhibition of NADH, pH 7.0, 25°C Saccharomyces cerevisiae
11.5
-
AMP linear uncompetitive inhibition of 2,6-dichlorophenolindophenol, pH 7.0, 25°C Saccharomyces cerevisiae