Lactate Dehydrogenase and its Isoenzymes

  • Shan S. Wong
Chapter
Part of the Pathology and Laboratory Medicine book series (PLM)

Abstract

Lactate dehydrogenase (EC 1.1.1.27; L-Lactate:NAD+ Oxidoreductase; LD)* belongs to the class of enzymes that catalyze oxidoreduction reactions and is widely distributed in all human tissues. It is involved in the last step of anaerobic glycolysis to regulate the pyruvate-lactate conversion for the replenishment of oxidized coenzyme, NAD+ (1–3). In the glycolytic pathway (Embden-Meyerhof), NAD+ is consumed with concomitant production of reduced nicotinamide adenine dinocleotide (NADH). LD catalyzes the of reduction of pyruvate to L-lactate with the mediation of NADH as a hydrogen donor. The reaction is reversible and strongly favors the production of lactate with an equilibrium constant of 3.6 × 104 M-l (4)

Keywords

Acute Myocardial Infarction Lactate Dehydrogenase Serum Enzyme Dehydrogenase Isoenzyme Creatine Kinase Isoenzyme 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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