Malic Dehydrogenase from porcine heart

Malic dehydrogenase exists as a dimer with each subunit containing an NAD-binding domain and a substrate-binding carboxy-terminal domain required for activity.

Malic dehydrogenase is a cytoplasmic isozyme and an important catalyst in the tricarboxylic acid cycle.

Malic Dehydrogenase is a ubiquitous enzyme, which exists in two isoforms in eukaryotic cells.

Malic dehydrogenase has been used in a study to assess the effect of an immunomodulator S2 complex on the enzymes of the parasites. It has also been used in a study to investigate the heterogeneity of lactic and malic dehydrogenase in cerebrospinal fluid.

Malic Dehydrogenase from porcine heart has been used:

• in qualitative protein binding measurements
• to test internally calibrated electrochemical continuous enzyme assay (ICECEA) with model enzyme pair
• to investigate the effect of chaperone on the refolding of heat-denatured malate dehydrogenase

Malic Dehydrogenase (MDH) plays an important role in the citric acid cycle in mitochondria. It catalyzes the interconversion of substrates malate and oxaloacetate with the simultaneous oxidation/reduction of NAD/NADH⁺. MDH present in the cytosol is involved in the shuttling of malate/aspartate.

Suspension in 2.8 M (NH₄)₂SO₄ solution, pH 6.0

One unit will convert 1.0 μmole of oxalacetate and β-NADH to L-malate and β-NAD per min at pH 7.5 at 25°C.