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Literature summary for 1.11.1.5 extracted from
- Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules (2006), Biochemistry, 45, 14371-14378.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K12C | characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound and located 90° from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase | Saccharomyces cerevisiae |
| K264C | characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound and located 90° from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase | Saccharomyces cerevisiae |
| N78C | characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound and located 90° from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase | Saccharomyces cerevisiae |
| V5C | characterization of complex with yeast cytochrome c mutant K79C. Cytochrome c is covalently bound via disulfide formation of the mutated residues and located on the back-side of the enzyme, 180° from its primary binding site. Catalytic activity is similar to wild-type cytochrome c peroxidase. Significant electrostatic repulsion of the two cytochrome c molecules bound in an 2:1 complex which decreases as the ionic strength of buffer increases | Saccharomyces cerevisiae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
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Release 2023.1 (January 2023)
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