Protein Variants | Comment | Organism |
---|---|---|
188K/P217L | mutation is introduced into yeast COX10 and tested in cox10DELTA cells. The double T188K/P217L mutant is unable to support respiratory growth, and cytochrome c oxidase activity in the mutant cells is markedly attenuated. Unstable mutant enzyme | Saccharomyces cerevisiae |
E328G | mutation is introduced into yeast COX10 and tested in cox10DELTA cells. The E328G Cox10 mutant supports respiratory growth and contributes to appreciable cytochrome c oxidase activity | Saccharomyces cerevisiae |
E328V | mutation is introduced into yeast COX10 and tested in cox10DELTA cells. Cells containing the E328V Cox10 are impaired in respiration and cytochrome c oxidase activity | Saccharomyces cerevisiae |
P217L | mutation is introduced into yeast COX10 and tested in cox10DELTA cells. The P217L Cox10 variant supports glycerol/lactate growth, but cytochrome c oxidase activity is slightly impaired | Saccharomyces cerevisiae |
T188K | mutation is introduced into yeast COX10 and tested in cox10DELTA cells. Cells harboring T188K Cox10 are partially compromised in respiratory growth. Mutant enzyme is unstable | Saccharomyces cerevisiae |
T188K/N196K | the double mutant exhibits no enhanced protein stability, and the cells are more compromised in glycerol/lactate growth and cytochrome c oxidase activity, compared with the single T188K mutant | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O | Saccharomyces cerevisiae | essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase | heme o + diphosphate | - |
? | |
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O | Saccharomyces cerevisiae ATCC 204508 | essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase | heme o + diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P21592 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | P21592 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O | - |
Saccharomyces cerevisiae | heme o + diphosphate | - |
? | |
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O | essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase | Saccharomyces cerevisiae | heme o + diphosphate | - |
? | |
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O | - |
Saccharomyces cerevisiae ATCC 204508 | heme o + diphosphate | - |
? | |
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O | essential enzyme for heme A formation. The synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase | Saccharomyces cerevisiae ATCC 204508 | heme o + diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
oligomer | the active state of Cox10 appears to be a homo-oligomeric complex, and formation of this complex is dependent on the newly synthesized CcO subunit Cox1 and the presence of an early Cox1 assembly intermediate. Cox10 multimerization is triggered by progression of Cox1 from the early assembly intermediate to downstream intermediates. The CcO assembly factor Coa2 appears important in coupling the presence of newly synthesized Cox1 to Cox10 oligomerization | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
Cox10 | - |
Saccharomyces cerevisiae |
heme o synthase | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
metabolism | the synthesis of the heme a cofactor used in cytochrome c oxidase is dependent on the sequential action of heme o synthase and heme a synthase | Saccharomyces cerevisiae |