One hallmark of cancer is altered cellular metabolism. Malic enzymes (MEs) are a family of homotetrameric enzymes that catalyse the reversible oxidative decarboxylation of L-malate to pyruvate, with a simultaneous reduction of NAD(P)+ to NAD(P)H. As MEs generate NADPH and NADH, they may play roles in energy production and reductive biosynthesis. Humans possess three ME isoforms; ME1 is cytosolic and utilises NADP+, ME3 is mitochondrial and can utilise NADP+ and ME2 is mitochondrial and can utililse either NAD+ or NADP+ (Chang & Tong 2003, Murugan & Hung 2012).NADP-dependent malic enzyme (ME1, aka c-NADP-ME) is a cytosolic enzyme that oxidatively decarboxylates (s)-malate (MAL) to pyruvate (PYR) and CO2 using NADP+ as cofactor (Zelewski & Swierczynski 1991). ME1 exists as a dimer of dimers (Murugan & Hung 2012, Hsieh et al. 2014) and a divalent metal such as Mg2+ is essential for catalysis (Chang & Tong 2003).
Tong, L, Chang, GG
Murugan, S, Hung, HC
Zelewski, M, Swierczyński, J
Li, SY, Chen, HY, Hung, HC, Yang, PC, Hsieh, JY, Chen, MC, Chan, NL, Liu, JH
malate dehydrogenase (decarboxylating) (NADP+) activity of ME1:Mg2+ tetramer [cytosol]
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