Lactate dehydrogenase is an enzyme that can:
• catalyzes the conversion of lactate to pyruvate and back, and
• converts NAD+ to NADH and back.
The reaction of lactate dehydrogenase usually occurs during a tissue damage. So, pyruvate, (the final product of glycolysis), is converted to lactate when oxygen is absent (in low concentration).
When the concentrations of lactate increases (as the product of lactate dehydrogenase reaction), the enzyme exhibits feedback inhibition (negative feedback).
The reactions catalyzed by lactate dehydrogenase in the skeletal muscles, liver, and heart are:
a. Catalyze the conversion of lactate to pyruvate and vice versa.
b. Reversible reduction of NAD+ to NADH.
LDH, or lactate dehydrogenase, is a key enzyme in the anaerobic metabolic process.
It is classified as an oxidoreductase and has the enzyme commission number EC 1.1. 1.27.
The enzyme works when we need more oxygen to perform chores, and the stored pyruvate is converted into oxygen.
When the concentration of lactate increase in the body due to heavy exersice or running the enzyme starts to work.
Thus, conversion of lactate to pyruvate and reduction of NAD+ to NADH+ re the reactions catalyzed by the enzyme.
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