Biochem/physiol Actions

L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD⁺ to NADH and H⁺. LDHA (L-lactate dehydrogenase A chain) is responsible for the conversion of pyruvate to lactate, the final step of glycolysis. It is overexpressed in various cancers. In cancer cells, HIF-1a (hypoxia-inducible factor) induces the expression of LDHA, which helps in maintaining glycolysis in cells.

L-lactic dehydrogenase catalyzes the conversion of L-lactate into L-pyruvate while reducing NAD⁺ to NADH and H⁺.

General description

L-lactate dehydrogenase (LDH) is an enzyme that catalyzes the conversion of lactate to pyruvate.In particular, lactic dehydrogenase A (LDHA) is mainly found in skeletal muscle, and for that reason is known as the M subunit. This recombinant form of LDHA has a C-terminal histidine-tag.The gene LDHA (L-lactate dehydrogenase A chain) is mapped to human chromosome 11p15. It is a subunit of lactate dehydrogenase.

Physical form

Buffered aqueous solution with Hepes (pH 7.5), NaCl and glycerol.

Unit Definition

One unit will reduce 1.0 µmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.