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Literature summary extracted from

  • Swenson, S.; Cannon, A.; Harris, N.J.; Taylor, N.G.; Fox, J.L.; Khalimonchuk, O.
    Analysis of oligomerization properties of heme a synthase provides insights into its function in eukaryotes (2016), J. Biol. Chem., 291, 10411-10425 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.17.99.9 R217W mutations of COX15 causing single amino acid conversions associated with fatal infantile hypertrophic cardiomyopathy and the neurological disorder Leigh syndrome results in impaired catalytic function, and the mutation affects oligomeric properties of the enzyme. The mutations affects protein folding and heme binding Saccharomyces cerevisiae
1.17.99.9 S344P mutations of COX15 causing single amino acid conversions associated with fatal infantile hypertrophic cardiomyopathy and the neurological disorder Leigh syndrome results in impaired stability. The mutations affect protein folding and heme binding Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.17.99.9 mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Organism

EC Number Organism UniProt Comment Textmining
1.17.99.9 Saccharomyces cerevisiae
-
-
-

Subunits

EC Number Subunits Comment Organism
1.17.99.9 multimer Cox15 exhibits homotypic interactions, forming highly stable complexes dependent upon hydrophobic interactions. This multimerization is evolutionarily conserved and independent of heme levels and heme a synthase catalytic activity. Cox15 multimerization is important for heme a biosynthesis and/or transfer to maturing cytochrome c oxidase Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.17.99.9 COX15
-
 Saccharomyces cerevisiae