MDH2 Human

MDH2 catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system . This reaction is a key step in the citric acid cycle, facilitating the conversion of energy stored in carbohydrates, fats, and proteins into ATP, the energy currency of the cell .

The protein encoded by MDH2 exists as a dimer, with each subunit containing two distinct domains: the NAD-binding domain and the catalytic domain . The NAD-binding domain is located in the amino-terminal half of each molecule and features a parallel-sheet structure known as the Rossmann fold motif .

MDH2 is localized to the mitochondria and is highly expressed in tissues with high energy demands, such as the heart, pancreas, small intestine, and adrenal system . It plays a pivotal role in the malate-aspartate shuttle, which is essential for the metabolic coordination between the cytosol and mitochondria .

Mutations in the MDH2 gene have been associated with various diseases, including developmental and epileptic encephalopathy 51 and hereditary paraganglioma-pheochromocytoma syndromes . These conditions highlight the importance of MDH2 in maintaining normal cellular function and energy metabolism.

Human recombinant MDH2 is produced using recombinant DNA technology, typically expressed in Escherichia coli (E. coli) to ensure high yield and purity . This recombinant form is used in various research applications, including studies on enzyme kinetics, metabolic pathways, and disease mechanisms.