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Biochemistry · Carbohydrate metabolism: gluconeogenesis regulation
Sample itemDuring prolonged fasting, hepatic beta-oxidation raises mitochondrial acetyl-CoA. Which enzyme is directly activated by acetyl-CoA to favour conversion of pyruvate to oxaloacetate?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
D. Pyruvate carboxylase
Pyruvate carboxylase is a biotin-dependent mitochondrial enzyme that is allosterically activated by acetyl-CoA. In fasting, acetyl-CoA from fatty acid oxidation therefore directs pyruvate towards oxaloacetate and gluconeogenesis rather than into the TCA cycle via acetyl-CoA. At the same time acetyl-CoA inhibits pyruvate dehydrogenase.
Option by option
A. Glucokinase
Glucokinase is induced by insulin and is not regulated by acetyl-CoA.
B. Pyruvate kinase
Pyruvate kinase is inhibited by alanine and by glucagon-mediated phosphorylation, not activated by acetyl-CoA.
C. Pyruvate dehydrogenase
Pyruvate dehydrogenase is inhibited by acetyl-CoA and NADH, which spares pyruvate for gluconeogenesis.
D. Pyruvate carboxylase (correct)
Correct. Acetyl-CoA is its specific allosteric activator.
Source note: Original NextPrep sample item — pending expert review. This item is original practice material awaiting independent expert review, so confirm important facts in a standard textbook.
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