Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | Cox10 is not affected by the presence/absence of its physiological partner, Cox15 | Saccharomyces cerevisiae |
General Stability | Organism |
---|---|
the stability of Cox10 is not decreased in the absence of cytochrome c oxidase | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrial membrane | inner | Saccharomyces cerevisiae | 31966 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P21592 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | P21592 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
Cox10 | - |
Saccharomyces cerevisiae |
heme o synthase | - |
Saccharomyces cerevisiae |
Organism | Comment | Expression |
---|---|---|
Saccharomyces cerevisiae | COX10 is regulated neither by intracellular heme B levels nor by Hap1 | additional information |
General Information | Comment | Organism |
---|---|---|
physiological function | the assembly and activity of cytochrome c oxidase is dependent on the availability of heme A, one of its essential cofactors. In eukaryotes, two inner mitochondrial membrane proteins, heme O synthase (Cox10) and heme A synthase (Cox15), are required for heme A biosynthesis. The two physiological partners do not share the same regulatory mechanism. The stoichiometry between Cox15 and Cox10 is 8:1, not 1:1 as it has generally been assumed | Saccharomyces cerevisiae |