Pyruvate, HCO3-, and ATP react to form oxaloacetate, ADP, and phosphate

Stable Identifier
Reaction [transition]
Homo sapiens
ATP + hydrogencarbonate + pyruvate => ADP + H(+) + oxaloacetate + phosphate
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Mitochondrial pyruvate carboxylase (PC) catalyzes the irreversible reaction of pyruvate, bicarbonate, and ATP to form oxaloacetate, ADP, phosphate, and H+. The enzyme is biotinylated and is active as a tetramer. Its structure and function have been characterized in detail (Jitrapakdee et al. 2008; Jitrapakdee & Wallace 1999), and both normal and defective forms of the human enzyme have been described (Carbone & Robinson 2003).

Literature References
PubMed ID Title Journal Year
18613815 Structure, mechanism and regulation of pyruvate carboxylase

Jitrapakdee, S, Rayment, I, Wallace, JC, St Maurice, M, Cleland, WW, Attwood, PV

Biochem J 2008
10229653 Structure, function and regulation of pyruvate carboxylase

Jitrapakdee, S, Wallace, JC

Biochem J 1999
12437512 Expression and characterization of a human pyruvate carboxylase variant by retroviral gene transfer

Robinson, BH, Carbone, MA

Biochem J 2003
Catalyst Activity

pyruvate carboxylase activity of PC tetramer [mitochondrial matrix]

This event is regulated
Positively by
Orthologous Events
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