LDHA Human

Lactate Dehydrogenase A (LDHA) is an enzyme that plays a crucial role in the metabolic pathway of glycolysis. It is responsible for the conversion of pyruvate, the end product of glycolysis, into lactate. This reaction is essential for regenerating NAD+, which allows glycolysis to continue producing ATP under anaerobic conditions .

LDHA is a member of the lactate dehydrogenase family and is encoded by the LDHA gene. The enzyme is composed of four subunits, forming a tetramer. Each subunit has a molecular weight of approximately 36 kDa . The active site of LDHA binds to pyruvate and NADH, facilitating the reduction of pyruvate to lactate and the oxidation of NADH to NAD+ .

A hallmark of many cancer cells is their altered metabolism, which involves a shift to aerobic glycolysis, also known as the Warburg effect. In this metabolic pathway, cancer cells preferentially convert glucose to lactate even in the presence of oxygen. LDHA is a key enzyme in this process, as it catalyzes the formation of lactate from pyruvate . This shift allows cancer cells to generate energy and biosynthetic precursors rapidly, supporting their rapid proliferation .

Recombinant human LDHA is produced using Escherichia coli expression systems. The recombinant protein is typically purified to high levels of purity, often exceeding 95% as determined by SDS-PAGE . It is used in various research applications, including studies on cancer metabolism, enzyme kinetics, and drug development.

Recombinant LDHA is widely used in biochemical assays to study its enzymatic activity and inhibition. It is also employed in structural biology to determine the three-dimensional structure of the enzyme and its complexes with inhibitors. Additionally, recombinant LDHA is used in drug discovery programs aimed at developing inhibitors that can target the enzyme and potentially treat cancers that rely on aerobic glycolysis .