Pyruvate dehydrogenase complex react with pyruvate to form acetyl-CoA
In prokaryotes, the pyruvate dehydrogenase complex is located in the cytoplasm.
Alpha-ketoglutarate dehydrogenase is the most similar to Pyruvate dehydrogenase because both are part of the α-ketoglutarate dehydrogenase complex, involved in the citric acid cycle and share structural and functional similarities.
Pyruvate dehydrogenase is typically found in the mitochondria of eukaryotic cells. It plays a critical role in the conversion of pyruvate into acetyl-CoA, a key step in the process of aerobic respiration.
Pyruvate dehydrogenase (PDH) are regulated by pyruvate dehydrogenase kinase (PDH-K) and PDH phosphatase. PDH-K effect on PDH is that it will inactivate PDH and PDH phosphatase will reactivate PDH. PDH-K is regulated by energy surpluses (ATP, NADH) and energy deficits (ADP, NAD). So when there is an energy surplus, PDH-K will inhibit PDH, and vice versa. PDH phosphatase will activate PDH and is upregulated by magnesium and calcium.
The products of acetyl CoA formation from a molecule of pyruvate are acetyl CoA, NADH, and carbon dioxide. This process occurs during the mitochondrial pyruvate dehydrogenase complex reaction, where pyruvate is converted to acetyl CoA by a series of enzymatic reactions.
In prokaryotes, the pyruvate dehydrogenase complex is located in the cytoplasm.
The enzyme that converts pyruvate into acetyl-CoA is pyruvate dehydrogenase. This multienzyme complex is responsible for catalyzing the conversion of pyruvate into acetyl-CoA, which is a key step in the metabolism of carbohydrates to produce energy.
Alpha-ketoglutarate dehydrogenase is the most similar to Pyruvate dehydrogenase because both are part of the α-ketoglutarate dehydrogenase complex, involved in the citric acid cycle and share structural and functional similarities.
Pyruvate dehydrogenase is typically found in the mitochondria of eukaryotic cells. It plays a critical role in the conversion of pyruvate into acetyl-CoA, a key step in the process of aerobic respiration.
Pyruvate dehydrogenase complex
Pyruvate dehydrogenase (PDH) are regulated by pyruvate dehydrogenase kinase (PDH-K) and PDH phosphatase. PDH-K effect on PDH is that it will inactivate PDH and PDH phosphatase will reactivate PDH. PDH-K is regulated by energy surpluses (ATP, NADH) and energy deficits (ADP, NAD). So when there is an energy surplus, PDH-K will inhibit PDH, and vice versa. PDH phosphatase will activate PDH and is upregulated by magnesium and calcium.
Correct answer: I, II, III and IV
The products of acetyl CoA formation from a molecule of pyruvate are acetyl CoA, NADH, and carbon dioxide. This process occurs during the mitochondrial pyruvate dehydrogenase complex reaction, where pyruvate is converted to acetyl CoA by a series of enzymatic reactions.
Dehydrogenase enzymes catalyze the removal of hydrogen atoms from a substrate molecule. This is an important step in various metabolic processes as it helps in transferring electrons and energy between molecules.
Thiamine pyrophosphate (TPP)
Pyruvate oxidation takes place in the mitochondrial matrix. Here, pyruvate is converted into acetyl-CoA by the pyruvate dehydrogenase complex, which is a critical step in aerobic respiration.
Enzymes that are involved in the breakdown of pyruvate include pyruvate dehydrogenase complex (PDC) and pyruvate carboxylase. These enzymes are crucial in converting pyruvate into acetyl-CoA to enter the citric acid cycle for further energy production.