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Literature summary extracted from

  • Hano, N.; Nakashima, Y.; Shinzawa-Itoh, K.; Yoshikawa, S.
    Effect of the side chain structure of coenzyme Q on the steady state kinetics of bovine heart NADH:coenzyme Q oxidoreductase (2003), J. Bioenerg. Biomembr., 35, 257-265.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.2 additional information
-
 additional information Km-value for NADH, decylubiquinone, coenzyme Q1 and coenzyme Q2 are measured at different concentrations of the cosubstrate Bos taurus

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
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.2 NADH + decylubiquinone
-
 Bos taurus NAD+ + decylubiquinol
-
 ?
7.1.1.2 NADH + H+ + coenzyme Q1
-
 Bos taurus NAD+ + reduced coenzyme Q1
-
 ?
7.1.1.2 NADH + H+ + coenzyme Q2
-
 Bos taurus NAD+ + reduced coenzyme Q2
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.2 NADH binding to the enzyme results in a conformational change, in the coenzyme Q binding site, which enables the site to accept coenzyme Q with a side chain significantly larger than one isoprenoid unit Bos taurus