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Literature summary extracted from

  • Lederer, F.
    Another look at the interaction between mitochondrial cytochrome c and flavocytochrome b 2 (2011), Eur. Biophys. J., 40, 1283-1299.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.2.3 Fcb2 free and in complex with sulfite, X-ray diffraction structure analysis at 2.3-2.6 A resolution Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.2.3 0.0015
-
 ferricytochrome c pH 7.5, 25°C, Tris-HCl buffer, mutant Y143F Saccharomyces cerevisiae
1.1.2.3 0.01
-
 ferricytochrome c pH 7.5, 25°C, Tris-HCl buffer, wild-type enzyme Saccharomyces cerevisiae
1.1.2.3 0.045
-
 ferricytochrome c pH 7.0, 5°C, phosphate buffer, wild-type enzyme Saccharomyces cerevisiae
1.1.2.3 0.121
-
 ferricytochrome c pH 7.0, 30°C, phosphate buffer, mutant Y143F Saccharomyces cerevisiae
1.1.2.3 0.131
-
 ferricytochrome c pH 7.0, 30°C, phosphate buffer, wild-type enzyme Saccharomyces cerevisiae
1.1.2.3 0.131
-
 ferricytochrome c pH 7.0, 5°C, phosphate buffer, mutant Y143F Saccharomyces cerevisiae
1.1.2.3 0.19
-
 (S)-lactate pH 7.5, 25°C, Tris-HCl buffer, mutant Y143F, with heme Saccharomyces cerevisiae
1.1.2.3 0.4
-
 (S)-lactate pH 7.0, 5°C, phosphate buffer, mutant Y143F, with heme Saccharomyces cerevisiae
1.1.2.3 0.53
-
 (S)-lactate pH 7.5, 25°C, Tris-HCl buffer, wild-type enzyme, with heme Saccharomyces cerevisiae
1.1.2.3 0.54
-
 (S)-lactate pH 7.0, 5°C, phosphate buffer, wild-type enzyme, with heme Saccharomyces cerevisiae
1.1.2.3 0.84
-
 (S)-lactate pH 7.5, 25°C, Tris-HCl buffer, wild-type enzyme, with FMN Saccharomyces cerevisiae
1.1.2.3 0.89
-
 (S)-lactate pH 7.0, 5°C, phosphate buffer, wild-type enzyme, with FMN Saccharomyces cerevisiae
1.1.2.3 2.5 5 (S)-lactate pH 7.0, 5°C, phosphate buffer, mutant Y143F, with FMN Saccharomyces cerevisiae
1.1.2.3 2.81
-
 (S)-lactate pH 7.5, 25°C, Tris-HCl buffer, mutant Y143F, with FMN Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.2.3 mitochondrial intermembrane space
-
 Saccharomyces cerevisiae 5758
-
1.1.2.3 soluble
-
 Saccharomyces cerevisiae
-
-

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.2.3 (S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+ catalytic cycle, overview Saccharomyces cerevisiae
a

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+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.2.3 homotetramer each subunit of the soluble tetrameric enzyme consists of an N-terminal b5-like heme-binding domain and a C terminal flavodehydrogenase. The first 99 residues are folded around the heme, the next about 390 constitute the FMN-binding domain, and the last residues up to 511 make contacts with the other three subunits. Thus, the flavodehydrogenase domains constitute the core of the molecule, with a fourfold symmetry, while the heme domains lie at the periphery Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.1.2.3 Fcb2
-
 Saccharomyces cerevisiae
1.1.2.3 flavocytochrome b2
-
 Saccharomyces cerevisiae
1.1.2.3 L-lactate ferricytochrome C oxidoreductase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.2.3 25 30 assay at 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 0.011
-
 ferricytochrome c pH 7.5, 25°C, Tris-HCl buffer, mutant Y143F Saccharomyces cerevisiae
1.1.2.3 0.103
-
 ferricytochrome c pH 7.5, 25°C, Tris-HCl buffer, wild-type enzyme Saccharomyces cerevisiae
1.1.2.3 20
-
 ferricytochrome c pH 7.0, 5°C, phosphate buffer, mutant Y143F Saccharomyces cerevisiae
1.1.2.3 61
-
 ferricytochrome c pH 7.0, 30°C, phosphate buffer, mutant Y143F Saccharomyces cerevisiae
1.1.2.3 61
-
 ferricytochrome c pH 7.0, 5°C, phosphate buffer, wild-type enzyme Saccharomyces cerevisiae
1.1.2.3 155
-
 ferricytochrome c pH 7.0, 30°C, phosphate buffer, wild-type enzyme Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.2.3 7 7.5 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.3 ferricytochrome c
-
 Saccharomyces cerevisiae
1.1.2.3 FMN flavohemoprotein, in the crystal structure, FMN and heme are face to face, and appear to be in a suitable orientation and at a suitable distance for exchanging electrons Saccharomyces cerevisiae
1.1.2.3 heme flavohemoprotein, in the crystal structure, FMN and heme are face to face, and appear to be in a suitable orientation and at a suitable distance for exchanging electrons. But in one subunit out of two, the heme domain is disordered and invisible. The heme domains are mobile in solution Saccharomyces cerevisiae
1.1.2.3 additional information binding studies and models of the complex between cytochrome c and Fcb2, E63 is involved in the interaction with cyt. c, overview. Cytochrome c mutants E63K/D72K and E63K/D72K show reduced activity, but neither the K296M nor the Y97F mutation show significantly alteration of the enzyme kinetics. Effect of mutations on heme and cytochrome binding, overview Saccharomyces cerevisiae