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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.

propionyl-CoA + CO2 + ATP D-methylmalonyl-CoA + ADP + orthophosphate

PROP-CoA + ATP + HCO3- → MEMA-CoA + ADP + Pi + H+

Reactome: R-HSA-71031
Compartment: mitochondrial matrix
Rhea: RHEA:23721

Inputs

PROP-CoACHEBI:57392, C24H36N7O17P3S, mitochondrial matrix
ATPCHEBI:30616, C10H12N5O13P3, mitochondrial matrix
HCO3-CHEBI:17544, CHO3, mitochondrial matrix

Outputs

MEMA-CoACHEBI:57327, C25H35N7O19P3S, mitochondrial matrix
ADPCHEBI:456216, C10H12N5O10P2, mitochondrial matrix
PiCHEBI:43474, HO4P, mitochondrial matrix
H+CHEBI:15378, H, mitochondrial matrix

Catalysed by

propionyl-CoA carboxylase activity of 6x(Btn-PCCA:PCCB) [mitochondrial matrix]EC 6.4.1.3

Literature

Isolation and characterization of propionyl-CoA carboxylase from normal human liver. Evidence for a protomeric tetramer of nonidentical subunits J Biol Chem, 1980
Metabolism of propionic acid in animal tissues. VIII. Crystalline propionyl carboxylase J Biol Chem, 1961
Mitochondrial targeting signals and mature peptides of 3-methylcrotonyl-CoA carboxylase Biochem Biophys Res Commun, 2005