phosphoenolpyruvate + ADP => pyruvate + ATP

Stable Identifier
Reaction [transition]
Homo sapiens
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Cytosolic pyruvate kinase catalyzes the transfer of a high-energy phosphate from phosphoenolpyruvate to ADP, forming pyruvate and ATP. This reaction, an instance of substrate-level phosphorylation, is essentially irreversible under physiological conditions.

Four isozymes of human pyruvate kinase have been described, L, R, M1 and M2. Isozymes L and R are encoded by alternatively spliced transcripts of the PKLR gene; isozymes M1 and M2 are encoded by alternatively spliced transcripts of PKM2. In the body, L pyruvate kinase is found in liver (Tani et al. 1988), R in red blood cells (Kanno et al. 1991), M1 in muscle, heart and brain (Takenaka et al. 1991), and M2 in early fetal tissues and tumors (e.g., Lee et al. 2008). In all cases, the active form of the enzyme is a homotetramer, activated by fructose 1,6-bisphosphate (Valentini et al. 2002; Dombrauckas et al. 2005). Mutations in PKLR have been associated with hemolytic anemias (e.g., Zanella et al. 2005).

Literature References
PubMed ID Title Journal Year
15996096 Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis

Dombrauckas, JD, Santarsiero, BD, Mesecar, AD

Biochemistry 2005
11960989 Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia

Dolzan, M, Bianchi, P, Mattevi, A, Abraham, DJ, Zanella, A, Fortin, R, Galizzi, A, Valentini, G, Wang, C, Chiarelli, LR

J Biol Chem 2002
15982340 Red cell pyruvate kinase deficiency: molecular and clinical aspects

Bianchi, P, Fermo, E, Zanella, A, Valentini, G

Br J Haematol 2005
18191611 Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription

Kim, J, Han, YM, Lee, J, Kim, HK

Int J Biochem Cell Biol 2008
3126495 Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells

Miwa, S, Nagata, S, Fujii, H, Tani, K

Proc Natl Acad Sci U S A 1988
2040271 Isolation and characterization of the human pyruvate kinase M gene

Matsuda, T, Noguchi, T, Hirai, H, Takenaka, M, Imai, E, Yamada, K, Tanaka, T, Sadahiro, S

Eur J Biochem 1991
1896471 cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia

Miwa, S, Fujii, H, Kanno, H, Hirono, A

Proc Natl Acad Sci U S A 1991
Catalyst Activity

pyruvate kinase activity of pyruvate kinase tetramer [cytosol]

This event is regulated
Negatively by