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Literature summary extracted from

  • Nakashima, Y.; Shinzawa-Itoh, K.; Watanabe, K.; Naoki, K.; Hano, N.; Yoshikawa, S.
    Steady-state kinetics of NADH:coenzyme Q oxidoreductase isolated from bovine heart mitochondria (2002), J. Bioenerg. Biomembr., 34, 11-19.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.2 NAD+ product inhibition Bos taurus
7.1.1.2 reduced coenzyme Q1 product inhibition Bos taurus
7.1.1.2 rotenone 150 nM, 85% inhibition in presence of 0.01 mM NADH, inhibition is independent of coenzyme Q1 concentration below 0.05 mM, rotenone sensitivity decreases significantly with coenzyme Q1 concentration above 0.1 mM Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.2 0.00172
-
NADH with 0.01 mM coenzyme Q1 Bos taurus
7.1.1.2 0.00195
-
NADH with 0.025 mM coenzyme Q1 Bos taurus
7.1.1.2 0.002
-
NADH with 0.05 mM coenzyme Q1 Bos taurus
7.1.1.2 0.0129
-
coenzyme Q1
-
Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.2 mitochondrion
-
Bos taurus 5739
-

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.2 Bos taurus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.1.1.2 heart
-
Bos taurus
-

Storage Stability

EC Number Storage Stability Organism
7.1.1.2 -80°C, 8-10 mg protein/ml, stable for at least 1 year Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.2 NADH + H+ + coenzyme Q1 ordered sequential mechanism in which the order of substrate binding and product release is coenzyme Q1, NADH, NAD+ and reduced coenzyme coenzyme Q1 Bos taurus NAD+ + reduced coenzyme Q1
-
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Synonyms

EC Number Synonyms Comment Organism
7.1.1.2 NADH:coenzyme Q oxidoreductase
-
Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.2 NADH
-
Bos taurus