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Pyruvate dehydrogenase deficiency (also known as pyruvate dehydrogenase complex deficiency or PDCD or PDH deficiency) is a rare neurodegenerative disorder associated with abnormal mitochondrial metabolism. PDCD is a genetic disease resulting from mutations in one of the components of the pyruvate dehydrogenase complex (PDC). [1]
The areas surrounding the phosphorylation sites on pyruvate dehydrogenase are shown in red. Pyruvate dehydrogenase kinase phosphorylation of these sites leads to decreased dehydrogenase activity. Pyruvate dehydrogenase directly follows the glycolytic pathway and is responsible for the conversion of pyruvate to acetyl-CoA which enters into the ...
[5] [6] It codes for an isozyme of pyruvate dehydrogenase kinase (PDK). Pyruvate dehydrogenase (PDH) is a part of a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals.
Pyruvate dehydrogenase (PDH) deficiency is a congenital degenerative metabolic disease resulting from a mutation of the pyruvate dehydrogenase complex (PDC) located on the X chromosome. While defects have been identified in all 3 enzymes of the complex, the E1-α subunit is predominantly the culprit.
The most common feature is a potentially life-threatening buildup of lactic acid (lactic acidosis), which can cause nausea, vomiting, severe breathing problems, and an abnormal heartbeat. People with pyruvate dehydrogenase deficiency usually have neurological problems as well.
Glycolysis breaks down glucose into pyruvate, which is then fermented to lactate; pyruvate flux through TCA cycle is down-regulated in cancer cells. Pathways branching off of glycolysis, such as the pentose phosphate pathway, generate biochemical building blocks to sustain the high proliferative rate of cancer cells.
Tumor M2-PK is produced in all rapidly dividing cells and is responsible for enabling cancer cells to consume glucose at an accelerated rate; on forcing the cells to switch to pyruvate kinase's alternative form by inhibiting the production of tumor M2-PK, their growth was curbed. The researchers acknowledged the fact that the exact chemistry of ...
Secondly, a proton must be added to the enolate of pyruvate to produce the functional form of pyruvate that the cell requires. [14] Because the substrate for pyruvate kinase is a simple phospho-sugar, and the product is an ATP, pyruvate kinase is a possible foundation enzyme for the evolution of the glycolysis cycle, and may be one of the most ...