D-lactate dehydrogenase

D-lactate dehydrogenase

Crystal structure of D-lactate dehydrogenase.

D-lactate dehydrogenase is an enzyme that plays a crucial role in the metabolism of D-lactic acid. It catalyzes the conversion of D-lactate to pyruvate, which is an important step in the glycolytic pathway. This enzyme is found in various organisms, including bacteria, fungi, and mammals.

Structure

The crystal structure of D-lactate dehydrogenase has been extensively studied. It consists of a single polypeptide chain that folds into a compact structure. The active site of the enzyme contains a cofactor called NAD+ (nicotinamide adenine dinucleotide), which is essential for the catalytic activity of the enzyme.

Function

D-lactate dehydrogenase plays a crucial role in the metabolism of D-lactic acid. It is involved in the conversion of D-lactate, a product of anaerobic glycolysis, to pyruvate. This reaction is important for the regeneration of NAD+ in the cell, which is required for the continuation of glycolysis.

Role in Health and Disease

D-lactate dehydrogenase is essential for maintaining the balance of D-lactic acid in the body. In humans, an imbalance in D-lactic acid levels can lead to a condition called D-lactic acidosis. This condition is characterized by the accumulation of D-lactic acid in the blood, which can result in symptoms such as abdominal pain, nausea, and neurological disturbances.

Clinical Significance

D-lactate dehydrogenase has been studied as a potential therapeutic target for various diseases. In particular, inhibitors of this enzyme have shown promise in the treatment of certain types of cancer. Additionally, mutations in the gene encoding D-lactate dehydrogenase have been associated with metabolic disorders, highlighting the importance of this enzyme in human health.

See Also

• Lactate dehydrogenase
• Glycolysis
• Metabolism