8. How and why are pyruvate kinase isozymes regulated differently? A. In the liver, dephosphorylation of pyruvate kinase is activated in response to high levels of fructose 1,6-bisphosphate B. In the liver, phosphorylation of pyruvate kinase diminishes its activity in response to low blood-glucose levels C. In the liver, activation of the GLUT2 receptors increases ATP synthesis leading to a decrease in pyruvate kinase activity D. In muscle, phosphorylation of pyruvate kinase diminishes its activity in response to low blood-glucose levels E. In muscle, dephosphorylation of pyruvate kinase is activated in response to high levels of fructose 1,6-bisphosphate9.Fermentation occurs in the absence of oxygen, but O2 is not found in any of the reactions of glycolysis or fermentation. So, what drives these reactions at the level of glycolysis and fermentation? A. In the formation of ethanol, acetaldehyde accepts electrons from NADH, regenerating NAD+ B. NADH synthesized in glycolysis is used to oxidize pyruvate to acetyl CoA during fermentation reactions C. ATP is synthesized in glycolysis, only if NAD+ is regenerated during fermentation D. In the formation of ethanol, pyruvate is decarboxylated in a reversible reaction, once oxygen is present again E. Pyruvate donates electrons to NADH in lactic acid fermentation
BCH 311 – How and why are pyruvate kinase isozymes
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