Lactate dehydrogenase (LDH) is an ubiquitous enzyme commonly found in wide variety of organisms, including plants and microbes. LDH is involved in the interconversion of the pyruvate and NADH to lactate and NAD+. It is also called Hydroxybutyrate Dehydrogenase (HBD), due to the fact that it can catalyze the oxidation of hydroxybutyrate (1). In mammals, three types of LDH subunits (35 kDa) are encoded by the genes Ldh-A, Ldh-B, and Ldh-C, forming various terameric isoenzymes (140 kDa). Lactate dehydrogenase A (LDH-A, muscle subunit, LDH-M) is involved in the final step of anaerobic glycoysis and catalyzes the conversion of L-lactate and NAD to pryruvate and NADH. While it is predominantly expressed in muscle tissue, it is hormonally regulated in rodents and overexpressed during mammary gland tumorigenesis (2). A mutation that cause deficiency in LDH-A has been implicated in exertional myoglobinuria (3).
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