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Information on EC 2.5.1.141 - heme o synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P21592

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IUBMB Comments
The enzyme, found in many archaea, bacteria, and eukaryotes, produces heme o, which in many cases is further modified into heme a. In organisms that produce heme a, the enzyme forms a complex with heme a synthase. In some archaeal species the enzyme transfers a geranylgeranyl group instead of a farnesyl group.
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Saccharomyces cerevisiae
UNIPROT: P21592
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cox10, heme o synthase, heme a:farnesyltransferase, protoheme ix farnesyltransferase, cyoe protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
protoheme IX farnesyltransferase
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:protoheme IX farnesyltranstransferase
The enzyme, found in many archaea, bacteria, and eukaryotes, produces heme o, which in many cases is further modified into heme a. In organisms that produce heme a, the enzyme forms a complex with heme a synthase. In some archaeal species the enzyme transfers a geranylgeranyl group instead of a farnesyl group.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
protoheme IX + (2E,6E)-farnesyl diphosphate + H2O
heme o + diphosphate
show the reaction diagram
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
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
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
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the stability of Cox10 is not decreased in the absence of cytochrome c oxidase
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
COX10 is regulated neither by intracellular heme B levels nor by Hap1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Biol. Chem.
284
839-847
2009
Saccharomyces cerevisiae (P21592), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P21592)
Manually annotated by BRENDA team
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
J. Biol. Chem.
287
26715-26726
2012
Saccharomyces cerevisiae (P21592), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P21592)
Manually annotated by BRENDA team