Malic Dehydrogenase from porcine heart

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

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 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 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 (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.