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Literature summary extracted from

  • Wang, Z.; Wang, Y.; Hegg, E.L.
    Regulation of the heme A biosynthetic pathway: differential regulation of heme A synthase and heme O synthase in Saccharomyces cerevisiae (2009), J. Biol. Chem., 284, 839-847.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.5.1.141 additional information Cox10 is not affected by the presence/absence of its physiological partner, Cox15 Saccharomyces cerevisiae

General Stability

EC Number General Stability Organism
2.5.1.141 the stability of Cox10 is not decreased in the absence of cytochrome c oxidase Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.5.1.141 mitochondrial membrane inner Saccharomyces cerevisiae 31966
-

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.141 Saccharomyces cerevisiae P21592
-
-
2.5.1.141 Saccharomyces cerevisiae ATCC 204508 P21592
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-

Synonyms

EC Number Synonyms Comment Organism
2.5.1.141 Cox10
-
 Saccharomyces cerevisiae
2.5.1.141 heme o synthase
-
 Saccharomyces cerevisiae

Expression

EC Number Organism Comment Expression
2.5.1.141 Saccharomyces cerevisiae COX10 is regulated neither by intracellular heme B levels nor by Hap1 additional information

General Information

EC Number General Information Comment Organism
2.5.1.141 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