ME1 tetramer decarboxylates OA to PYR

Stable Identifier
R-HSA-9861660
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Cytosolic malic enzyme (ME1, aka c-NADP-ME) oxidatively decarboxylates oxaloacetate (OA) to pyruvate (PYR). As the catalytic rate of this reaction is 5-25% of that of malate decarboxylation, its relevance is unclear ((Zelewski & Swierczyński, 1991; Bukato et al., 1995). ME1 exists as a dimer of dimers (Murugan & Hung, 2012; Hsieh et al., 2014), and a divalent metal such as Mg2+ or Mn2+ is essential for catalysis (Bukato et al., 1995; Chang & Tong, 2003).
Literature References
PubMed ID Title Journal Year
14596586 Structure and function of malic enzymes, a new class of oxidative decarboxylases

Tong, L, Chang, GG

Biochemistry 2003
23284632 Biophysical characterization of the dimer and tetramer interface interactions of the human cytosolic malic enzyme

Murugan, S, Hung, HC

PLoS ONE 2012
1935931 Malic enzyme in human liver. Intracellular distribution, purification and properties of cytosolic isozyme

Zelewski, M, Swierczyński, J

Eur. J. Biochem. 1991
24998673 Structural characteristics of the nonallosteric human cytosolic malic enzyme

Li, SY, Chen, HY, Hung, HC, Yang, PC, Hsieh, JY, Chen, MC, Chan, NL, Liu, JH

Biochim. Biophys. Acta 2014
7757881 Purification and properties of cytosolic and mitochondrial malic enzyme isolated from human brain

Bukato, G, Kochan, Z, Swierczyński, J

Int J Biochem Cell Biol 1995
Participants
Participates
Catalyst Activity

oxaloacetate decarboxylase activity of ME1 tetramer [cytosol]

Orthologous Events
Cross References
RHEA
Rhea
Authored
Reviewed
Created
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