propionyl-CoA + CO2 + ATP <=> D-methylmalonyl-CoA + ADP + orthophosphate

Stable Identifier
Reaction [transition]
Homo sapiens
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Propionyl CoA carboxylase in the mitochondrial matrix catalyzes the reaction of propionyl-CoA, CO2, and ATP to form D-methylmalonyl-CoA, ADP, and orthophosphate. The active form of the enzyme is a heteromultimer, probably consisting of six alpha subunits each bound to a biotin molecule and six beta subunits (Kaziro et al. 1961; Kalousek et al. 1980; Fenton et al. 2001). Both alpha and beta subunits are posttranslationally modified to remove amino-terminal mitochondrial import sequences (Stadler et al. 2005).

Literature References
PubMed ID Title Journal Year
6765947 Isolation and characterization of propionyl-CoA carboxylase from normal human liver. Evidence for a protomeric tetramer of nonidentical subunits

Kalousek, F, Darigo, MD, Rosenberg, LE

J Biol Chem 1980
  The Metabolic and Molecular Bases of Inherited Disease, 8th ed

Scriver, CR, Beaudet, AL, Valle, D, Sly, WS

16023992 Mitochondrial targeting signals and mature peptides of 3-methylcrotonyl-CoA carboxylase

Stadler, SC, Polanetz, R, Meier, S, Mayerhofer, PU, Herrmann, JM, Anslinger, K, Roscher, AA, Röschinger, W, Holzinger, A

Biochem Biophys Res Commun 2005
13752080 Metabolism of propionic acid in animal tissues. VIII. Crystalline propionyl carboxylase

Kaziro, Y, Ochoa, S, Warner, RC, Chen, JY

J Biol Chem 1961
Participant Of
Catalyst Activity
Catalyst Activity
propionyl-CoA carboxylase activity of 6x(Btn-PCCA:PCCB) [mitochondrial matrix]
Physical Entity
Orthologous Events
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