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Pyruvate dehydrogenase is an enzyme that catalyzes the reaction of pyruvate and a lipoamide to give the acetylated dihydrolipoamide and carbon dioxide The flux through pdc is tightly regulated in tissues under different metabolic conditions. The conversion requires the coenzyme thiamine pyrophosphate.
Dihydrolipoyl dehydrogenase which uses flavin adenine dinucleotide (fad) as its cofactor In mammals, pdc plays the role of a gatekeeper in the metabolism of pyruvate to maintain glucose homeostasis during the fed and fasting states Pyruvate dehydrogenase complex (pdc) deficiency is a type of metabolic disease
This means that the body is not able to efficiently break down nutrients in food to be used for energy
Symptoms of pdc deficiency include signs of metabolic dysfunction such as extreme tiredness (lethargy), poor feeding, and rapid breathing (tachypnea) Other symptoms may include signs of neurological dysfunction. Pyruvate dehydrogenase (pdh) is an enzyme complex that plays a role in cellular metabolism It serves as a bridge, connecting glycolysis, which breaks down glucose, to the citric acid cycle, a central pathway for energy production.
Pyruvate dehydrogenase kinases (pdks) can regulate the conversion of pyruvate to acetyl coenzyme a through the mitochondrial pyruvate dehydrogenase complex (pdhc)
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