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Literature summary for 1.1.2.3 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)

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

KM Value [mM]

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25 30 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.011
-
ferricytochrome c pH 7.5, 25°C, Tris-HCl buffer, mutant Y143F Saccharomyces cerevisiae
0.103
-
ferricytochrome c pH 7.5, 25°C, Tris-HCl buffer, wild-type enzyme Saccharomyces cerevisiae
20
-
ferricytochrome c pH 7.0, 5°C, phosphate buffer, mutant Y143F Saccharomyces cerevisiae
61
-
ferricytochrome c pH 7.0, 30°C, phosphate buffer, mutant Y143F Saccharomyces cerevisiae
61
-
ferricytochrome c pH 7.0, 5°C, phosphate buffer, wild-type enzyme Saccharomyces cerevisiae
155
-
ferricytochrome c pH 7.0, 30°C, phosphate buffer, wild-type enzyme Saccharomyces cerevisiae

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ferricytochrome c
-
Saccharomyces cerevisiae
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
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
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