Biochemistry, Lactate Dehydrogenase
Aisha Farhana, Sarah L. Lappin
Abstract
Lactate dehydrogenase (LDH) is an important enzyme of the anaerobic metabolic pathway. It belongs to the class of oxidoreductases, with an enzyme commission number EC 1.1.1.27. The function of the enzyme is to catalyze the reversible conversion of lactate to pyruvate with the reduction of NAD+ to NADH and vice versa. The enzyme is present in a variety of organisms, that include plants and animals. It is ubiquitously present in all tissues and serves as an important checkpoint of gluconeogenesis and DNA metabolism. A species-wide analysis of LDH demonstrates its well-preserved structure with only a few changes in the amino acid sequence across species. The structural similarity with slight amino acid changes provides a logical platform for designing functional molecules to modulate the catalytic potential and expression of the enzyme. This article will focus on the biochemical function, testing methods, and clinical relevance of the LDH enzyme.