LACTATE DEHYDROGENASE: STRUCTURE, FUNCTIONS AND ITS SIGNIFICANCE

Lactate dehydrogenase (E.C. 1.1.1.27) is an oligomeric enzyme of class oxidoreductase with systematic name, L-Lactate: NAD+ Oxidoreductase. It catalyzes the conversion of Lactate to pyruvate with production of reduced coenzyme, Nicotinamide adenine dinucleotide. It is a tetramer of 140,000 MW and its three dimensional structure and active site has been described. Its isoenzymes LDH-1, LDH-2, LDH-3, LDH-4, LDH-5 and LDH-C has been distributed in different human tissues which include skeletal muscle, heart, kidney, liver, spleen, lungs, erythrocytes, platelets, white blood cells and brain. Oncogenic signals has increased the expression of ldh-a genes in cancerous cells. Lactate dehydrogenase inhibition can be used as an anticancer therapy. LDH is an important diagnostic marker for hemolytic anemia and a couple of other diseases. It has its applications in lactate biosensors as well.