In the presence of a higher concentration of acetyl-CoA, the speed of the pyruvate dehydrogenase-catalyzed reaction is slower.
Pyruvate dehydrogenase is an enzyme that initiates the reaction of pyruvate and a lipoamide to produce acetylated dihydrolipoamide and CO2. The coenzyme thiamine pyrophosphate is required for the conversion.
Pyruvate dehydrogenase (PDH) is a key regulator of metabolic fine-tuning among glucose and FA oxidation. As a result, PDH transforms pyruvate to acetyl-coA, increasing the influx of acetyl-coA into the TCA cycle from glycolysis.
Acetyl-CoA reacts with oxaloacetate to start the citric acid cycle and make a significant contribution to energy production through aerobic metabolism. NADH, ATP, and acetyl-CoA all act as negative regulators of PDHC. The positive control of PHDC at pyruvate dehydrogenase contains insulin and Ca2+ influx.
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