Succinate dehydrogenase

Succinate dehydrogenase (SDH) is an enzyme that plays an important role in cellular energy metabolism. It is a key enzyme in the Krebs cycle, which is responsible for energy production in cells. LDH is involved in the oxidation of succinate to fumarate, which is the first step of the Krebs cycle.

Succinate dehydrogenase was discovered in 1941 and has since been the subject of numerous studies. It has been found to be of great importance for human and animal health. For example, lack of SDH can lead to various diseases such as diabetes, cancer and others.

In the body, succinate dehydrogenase is found in the mitochondria of cells, where it is involved in energy production. This enzyme also plays an important role in regulating glucose and fatty acid metabolism.

One of the main functions of succinate dehydrogenase is its ability to reduce coenzyme Q (CoQ), which is an important component of the mitochondrial respiratory chain. Decreased SDH activity can lead to CoQ deficiency, which can cause various diseases such as mitochondrial diseases.

Thus, succinate dehydrogenase is a key enzyme involved in cellular energy production and regulation of glucose and fatty acid metabolism. A deficiency of this enzyme can lead to various diseases and energy metabolism disorders.

Succinate dehydrogenase is an oxido-reductoase enzyme that catalyzes the oxidation of fumarate to malate. It plays an important role in the metabolism of carbohydrates, fatty acids and the synthesis of essential amino acids such as valine, leucine and threonine.

Succinate dehydrogenase is also known as fumarate kinase or succinate mishokinase. In its structure, it is a protein consisting of approximately 358 amino acid residues linked into two subunits connected by disulfide bridges. Each of the subunits has one domain containing the mitochondrial coenzyme Q-binding receptor. The function of these two domains is to catalyze the oxidation of fumarates, with the substrate accepting electrons from CoQ and converting fumarate to malate, representing the first step of glycolysis. In addition, succinatanase performs protective functions. At high concentrations of fumarates in the cytoplasm, it reduces the content of these low molecular weight compounds and, thereby, normalizes the level of oxygen in the cell. In some cases, deficiency of this enzyme leads to abnormally elevated levels of fumarics, which occurs in cases of metabolic disorders. Treatment of such diseases is carried out by introducing recombinant forms of enzymes. It is also worth noting that studies have confirmed the relationship of succinadenase with hereditary disorders of lipid metabolism, including disruption of cell structure as a result of the formation of fat-like substances due to mitochondrial disorders

Succinate dehydrogenase is an enzyme that catabolizes ethanol and produces acetyl-CoA. The main pathway of succinate catabolism in skeletal muscle mitochondria is the synthesis of ATP by oxidation of succinyl-CoA. In addition, succinylacetone can be formed from succinate by combination with acetylene, and can also be reduced to isobutylacetone or butanol through reductive carboxylation. These compounds are not part of normal metabolism, but may be of some interest as intermediates when succinates are used for the synthesis of other compounds.