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Literature summary for 7.1.1.2 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
Search for more literature for 7.1.1.2

Inhibitors

Inhibitors Comment Organism Structure
NAD+ product inhibition Bos taurus
reduced coenzyme Q1 product inhibition Bos taurus
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]

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

Localization

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Bos taurus
-

Storage Stability

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?

Synonyms

Synonyms Comment Organism
NADH:coenzyme Q oxidoreductase
-
 Bos taurus

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Bos taurus