LDHA Mouse

Lactate Dehydrogenase A (LDHA) is a crucial enzyme involved in the metabolic pathway of anaerobic glycolysis. It catalyzes the reversible conversion of pyruvate to lactate with the concomitant oxidation of NADH to NAD+. This enzyme is predominantly found in skeletal muscle and is part of the lactate dehydrogenase family .

LDHA is a protein-coding gene that encodes the A subunit of the lactate dehydrogenase enzyme. The enzyme is composed of four subunits, forming a tetrameric structure. Each subunit has a molecular weight of approximately 35 kDa, resulting in a total molecular weight of around 140 kDa for the tetrameric enzyme . The enzyme’s active site binds to pyruvate and NADH, facilitating the conversion to lactate and NAD+ under anaerobic conditions .

LDHA is predominantly expressed in muscle tissue, where it plays a vital role in energy production during intense physical activity. The expression of LDHA is hormonally regulated in rodents and is known to be overexpressed during mammary gland tumorigenesis . This overexpression is often associated with the altered glycolytic metabolism observed in cancer cells .

Recombinant LDHA from mice is produced using various expression systems, such as baculovirus. The recombinant protein typically includes a His-tag for purification purposes and corresponds to the amino acids 1-332 of the mouse LDHA sequence . The recombinant enzyme retains its functionality, with a specific activity of over 250 units/mg, defined as the amount of enzyme that converts 1.0 µmole of pyruvate to L-lactate per minute at pH 7.5 at 37°C .

Mutations in the LDHA gene have been linked to exertional myoglobinuria, a condition characterized by muscle pain and weakness following intense exercise . Additionally, LDHA is a potential target for cancer therapy due to its role in the altered glycolytic metabolism of cancer cells .