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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

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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

Select a territory to bring it forward.

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.

PC carboxylates PYR to OA

ATP + PYR + HCO3- → ADP + Pi + OA + H+

Reactome: R-HSA-70501
Compartment: mitochondrial matrix
Rhea: RHEA:20845

Inputs

ATPCHEBI:30616, C10H12N5O13P3, mitochondrial matrix
PYRCHEBI:15361, C3H3O3, mitochondrial matrix
HCO3-CHEBI:17544, CHO3, mitochondrial matrix

Outputs

ADPCHEBI:456216, C10H12N5O10P2, mitochondrial matrix
PiCHEBI:43474, HO4P, mitochondrial matrix
OACHEBI:16452, C4H2O5, mitochondrial matrix
H+CHEBI:15378, H, mitochondrial matrix

Catalysed by

pyruvate carboxylase activity of PC tetramer [mitochondrial matrix]EC 6.4.1.1

Literature

Expression and characterization of a human pyruvate carboxylase variant by retroviral gene transfer Biochem J, 2003
Structure, function and regulation of pyruvate carboxylase Biochem J, 1999
Structure, mechanism and regulation of pyruvate carboxylase Biochem J, 2008
Molecular characterization of pyruvate carboxylase deficiency in two consanguineous families Pediatr Res, 1998
CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase Nat Commun, 2022
Purification and properties of human liver pyruvate carboxylase Biochem Med, 1974