D-Lactic Dehydrogenase from Lactobacillus leichmannii

Research area: Cell Signalling D-lactate dehydrogenase belongs to the D-isomer-specific 2-hydroxyacid dehydrogenase family. Lactate dehydrogenase (LD) is a tetramer consisting of two (H and M) subunits. It has five isozymes (LD1 to LD5) and this composition varies in different tissues. LD1 is abundant in the kidney, heart, and erythrocytes. LD5 is found in the liver and skeletal muscles. LD is a ubiquitous molecule found in plants, yeast, mammals, and microorganisms and is a member of the oxidoreductase family.

Lactic dehydrogenase (LDH)plays an important role in the glycolytic pathway where it converts pyruvate tolactate by using NAD⁺ as a co-factor. It is considered animportant molecule that can be used in cancer therapy as it acts as aglycolytic inhibitor. Inhibition of LDH is associated with blocking of aerobicglycolysis in tumour cells.

One unit will reduce 1.0 μmole of pyruvate to D-lactate per min at pH 7.0 at 25 °C.

Suspension in 3.2 M (NH₄)₂SO₄, pH 6.0