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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

Data

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Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

Territories

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Reading the map

Metabolite; its structure appears as you zoom in
Reaction, arrow toward the product
Cofactors and co-substrates are written beside the reaction when you zoom in
Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

COX10 transforms heme to heme O

FPP + H2O + heme b → PPi + heme O

Reactome: R-HSA-2995330
Compartment: mitochondrial matrix · mitochondrial inner membrane
Rhea: None recorded

Inputs

FPPCHEBI:175763, C15H25O7P2, mitochondrial matrix
H2OCHEBI:15377, H2O, mitochondrial matrix
heme bCHEBI:26355, C34H32FeN4O4, mitochondrial inner membrane

Outputs

PPiCHEBI:33019, HO7P2, mitochondrial matrix
heme OCHEBI:60530, C49H56FeN4O5, mitochondrial inner membrane

Catalysed by

protoheme IX farnesyltransferase activity of COX10(?-443) [mitochondrial inner membrane]EC 2.5.1.141; UniProt Q12887

Literature

Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant Proc. Natl. Acad. Sci. U.S.A., 1994
Genomic structure and expression of the human heme A:farnesyltransferase (COX10) gene Genomics, 1997
Biosynthesis and trafficking of heme o and heme a : new structural insights and their implications for reaction mechanisms and prenylated heme transfer Crit Rev Biochem Mol Biol, 2021