Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.5.9 2,6-dichlorophenolindophenol substrate inhibition Saccharomyces cerevisiae
1.6.5.9 AMP dead end reversible inhibitor, competitive inhibitor of NADH and uncompetitive inhibitor of 2,6-dichlorophenolindophenol Saccharomyces cerevisiae
1.6.5.9 flavone partial inhibitor Saccharomyces cerevisiae
1.6.5.9 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
1.6.5.9 NADH substrate inhibition Saccharomyces cerevisiae
1.6.5.9 reduced 2,6-dichlorophenolindophenol product inhibition Saccharomyces cerevisiae
7.1.1.2 2,6-dichlorophenolindophenol
-
Saccharomyces cerevisiae
7.1.1.2 AMP dead-end inhibitor, linear competitive inhibitor of NADH, linear uncompetitive inhibitor of oxidized 2,6-dichlorophenol indophenol Saccharomyces cerevisiae
7.1.1.2 flavone dead-end inhibitor; partial inhibitor displaying a hyperbolic uncompetitive inhibition with respect to oxidized 2,6-dichlorophenol indophenol Saccharomyces cerevisiae
7.1.1.2 reduced 2,6-dichlorophenolindophenol
-
Saccharomyces cerevisiae
7.1.1.2 rotenone rotenone-insensitive enzyme Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.5.9 0.0062
-
2,6-dichlorophenolindophenol pH 7.0, 25°C Saccharomyces cerevisiae
1.6.5.9 0.0094
-
NADH pH 7.0, 25°C Saccharomyces cerevisiae
7.1.1.2 0.0062
-
oxidized 2,6-dichlorophenolindophenol
-
Saccharomyces cerevisiae
7.1.1.2 0.0094
-
NADH
-
Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.5.9 mitochondrion
-
Saccharomyces cerevisiae 5739
-
7.1.1.2 mitochondrion
-
Saccharomyces cerevisiae 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.5.9 53000
-
-
Saccharomyces cerevisiae
7.1.1.2 53000
-
x * 53000, SDS-PAGE Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.5.9 NADH + H+ + ubiquinone Saccharomyces cerevisiae
-
NAD+ + ubiquinol
-
?
7.1.1.2 NADH + ubiquinone Saccharomyces cerevisiae the enzyme catalyzes the transfer of electrons without translocation of protons across the membrane ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.6.5.9 Saccharomyces cerevisiae
-
-
-
7.1.1.2 Saccharomyces cerevisiae
-
rotenone-insensitive enzyme
-

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
7.1.1.2 NADH + ubiquinone + 6 H+[side 1] = NAD+ + ubiquinol + 7 H+[side 2] ping-pong mechanism Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.5.9 additional information the yeast enzyme is a two-electron reaction enzyme Saccharomyces cerevisiae ?
-
?
1.6.5.9 NADH + H+ + 2,6-dichlorophenolindophenol
-
Saccharomyces cerevisiae NAD+ + reduced 2,6-dichlorophenolindophenol
-
?
1.6.5.9 NADH + H+ + ubiquinone
-
Saccharomyces cerevisiae NAD+ + ubiquinol
-
?
7.1.1.2 NADH + oxidized 2,6-dichlorophenolindophenol
-
Saccharomyces cerevisiae NAD+ + reduced 2,6-dichlorophenolindophenol
-
?
7.1.1.2 NADH + oxidized 2,6-dichlorophenolindophenol + H+ 2,6-dichlorophenol indophenol as electron acceptor Saccharomyces cerevisiae NAD+ + reduced 2,6-dichlorophenolindophenol
-
?
7.1.1.2 NADH + ubiquinone
-
Saccharomyces cerevisiae NAD+ + ubiquinol
-
?
7.1.1.2 NADH + ubiquinone the enzyme catalyzes the transfer of electrons without translocation of protons across the membrane Saccharomyces cerevisiae ?
-
?
7.1.1.2 NADH + ubiquinone-6
-
Saccharomyces cerevisiae NAD+ + ubiquinol-6
-
?

Subunits

EC Number Subunits Comment Organism
7.1.1.2 ? x * 53000, SDS-PAGE Saccharomyces cerevisiae

Synonyms

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.5.9 6.5
-
-
Saccharomyces cerevisiae

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.6.5.9 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

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.6.5.9 0.0054
-
flavone hyperbolic uncompetitive inhibition of NADH, pH 7.0, 25°C Saccharomyces cerevisiae
1.6.5.9 0.0071
-
flavone hyperbolic noncompetitive inhibition of 2,6-dichlorophenolindophenol, pH 7.0, 25°C Saccharomyces cerevisiae
1.6.5.9 0.0141
-
reduced 2,6-dichlorophenolindophenol pH 7.0, 25°C Saccharomyces cerevisiae
1.6.5.9 0.0525
-
NADH pH 7.0, 25°C Saccharomyces cerevisiae
1.6.5.9 0.1152
-
2,6-dichlorophenolindophenol pH 7.0, 25°C Saccharomyces cerevisiae
1.6.5.9 5.5
-
AMP linear competitive inhibition of NADH, pH 7.0, 25°C Saccharomyces cerevisiae
1.6.5.9 11.5
-
AMP linear uncompetitive inhibition of 2,6-dichlorophenolindophenol, pH 7.0, 25°C Saccharomyces cerevisiae
7.1.1.2 0.015
-
2,6-dichlorophenolindophenol
-
Saccharomyces cerevisiae
7.1.1.2 5.5
-
AMP versus NADH Saccharomyces cerevisiae
7.1.1.2 11.5
-
AMP versus oxidized 2,6-dichlorophenolindophenol Saccharomyces cerevisiae