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Literature summary extracted from

  • Geier, B.M.; Schagger, H.; Ortwein, C.; Link, T.A.; Hagen, W.R.; Brandt, U.; Von Jagow, G.
    Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method (1995), Eur. J. Biochem., 227, 296-302.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.9 0.00132
-
 ferrocytochrome c horse heart cytochrome c, high-affinity Km, 30 mM ionic strength Saccharomyces cerevisiae
7.1.1.9 0.0153
-
 ferrocytochrome c horse heart cytochrome c, 100 mM ionic strength Saccharomyces cerevisiae
7.1.1.9 0.13
-
 ferrocytochrome c horse heart cytochrome c, low-affinity Km, 30 mM ionic strength Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.9 mitochondrial membrane
-
 Saccharomyces cerevisiae 31966
-

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.9 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.1.9 hydroxyapatite, Sepharose CL-6B Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.9 ferrocytochrome c + O2 horse ferrocytochrome c Saccharomyces cerevisiae ferricytochrome c + H2O
-
 ?
7.1.1.9 ferrocytochrome c + O2 + H+
-
 Saccharomyces cerevisiae ferricytochrome c + H2O
-
 r

Subunits

EC Number Subunits Comment Organism
7.1.1.9 More enzyme complex contains eleven rather than twelve subunits Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.1.1.9 1500
-
 ferrocytochrome c horse heart cytochrome c Saccharomyces cerevisiae