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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrial intermembrane space | - |
Saccharomyces cerevisiae | 5758 | - |
soluble | - |
Saccharomyces cerevisiae | - |
- |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+ | catalytic cycle, overview | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-lactate + 2 ferricytochrome c | - |
Saccharomyces cerevisiae | pyruvate + 2 ferrocytochrome c + 2 H+ | - |
? |
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 | Comment | Organism |
---|---|---|
Fcb2 | - |
Saccharomyces cerevisiae |
flavocytochrome b2 | - |
Saccharomyces cerevisiae |
L-lactate ferricytochrome C oxidoreductase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 30 | assay at | Saccharomyces cerevisiae |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | 7.5 | assay at | Saccharomyces cerevisiae |
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 |