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Literature summary for 2.5.1.141 extracted from

  • Khalimonchuk, O.; Kim, H.; Watts, T.; Perez-Martinez, X.; Winge, D.R.
    Oligomerization of heme o synthase in cytochrome oxidase biogenesis is mediated by cytochrome oxidase assembly factor Coa2 (2012), J. Biol. Chem., 287, 26715-26726.
    View publication on PubMedView publication on EuropePMC

Protein Variants

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/ Products (Substrates)

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
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?
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
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?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P21592
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Saccharomyces cerevisiae ATCC 204508 P21592
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
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Saccharomyces cerevisiae heme o + diphosphate
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?
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

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

Synonyms Comment Organism
Cox10
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Saccharomyces cerevisiae
heme o synthase
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Saccharomyces cerevisiae

General Information

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