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Literature summary extracted from

  • Daff, S.; Sharp, R.E.; Short, D.M.; Bell, C.; White, P.; Manson, F.D.; Reid, G.A.; Chapman, S.K.
    Interaction of cytochrome c with flavocytochrome b2 (1996), Biochemistry, 35, 6351-6357.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.2.3 E91K mutation has no effect on the rate of cytochrome c reduction, no significantly different behavior with regard to inhibition by ferrocytochrome c Saccharomyces cerevisiae
1.1.2.3 F52A mutation has no effect on the rate of cytochrome c reduction Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.2.3 Ferrocytochrome
-
 Saccharomyces cerevisiae
1.1.2.3 zinc-substituted cytochrome c
-
 Saccharomyces cerevisiae

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.2.3 (S)-lactate + 2 ferricytochrome c
-
 Saccharomyces cerevisiae pyruvate + 2 ferrocytochrome c + 2 H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.2.3 flavocytochrome b2
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.2.3 additional information
-
 additional information second-order rate constant for cytochrome c reduction in the pre-steady-state determined by stopped-flow spectrophotometry Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.2.3 0.006
-
 Ferrocytochrome pH 7.5, 25°C, mutant enzyme E91K Saccharomyces cerevisiae
1.1.2.3 0.0073
-
 zinc-substituted cytochrome c pH 7.5, 25°C, wild-type enzyme Saccharomyces cerevisiae
1.1.2.3 0.0088
-
 Ferrocytochrome pH 7.5, 25°C, wild-type enzyme Saccharomyces cerevisiae