If the serine phosphorylated by Protein Kinase A (PKA) on phosphofructokinase-2 (PFK2) were mutated to an aspartate, how might this affect gluconeogenesis in the liver? O The rate of gluconeogenesis would be unchanged, since PKA would be unable to inhibit the formation of fructose-2,6- bisphosphate through phosphorylation of PFK2. O The rate of gluconeogenesis would increase, since PKA would phosphorylate an aspartate instead of a serine residue on PFK2, which would inhibit the formation of fructose-2,6-bisphosphate. O The rate of gluconeogenesis would increase, since PKA would phosphorylate an aspartate instead of a serine residue on PFK2, which would activate the formation of fructose-2,6-bisphosphate. O The rate of gluconeogenesis would be diminished, since PKA would phosphorylate an aspartate instead of a serine residue on PFK2, which would inhibit the formation of fructose-2,6-bisphosphate. O The rate of gluconeogenesis would be diminished, since PKA would be unable to inhibit the formation of fructose-2,6- bisphosphate through phosphorylation of PFK2.

Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter25: Nitrogen Acquisition And Amino Acid Metabolism
Section: Chapter Questions
Problem 16P: A Deficiency on 3-Phosphogtycerate Dehydrogenase Can Affect Amino Acid Metabolism Although serine is...
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If the serine phosphorylated by Protein Kinase A (PKA) on phosphofructokinase-2 (PFK2) were mutated to an aspartate, how might
this affect gluconeogenesis in the liver?
O The rate of gluconeogenesis would be unchanged, since PKA would be unable to inhibit the formation of fructose-2,6-
bisphosphate through phosphorylation of PFK2.
O The rate of gluconeogenesis would increase, since PKA would phosphorylate an aspartate instead of a serine residue on
PEK2, which would inhibit the formation of fructose-2,6-bisphosphate.
O The rate of gluconeogenesis would increase, since PKA would phosphorylate an aspartate instead of a serine residue on
PFK2, which would activate the formation of fructose-2,6-bisphosphate.
O The rate of gluconeogenesis would be diminished, since PKA would phosphorylate an aspartate instead of a serine
residue on PFK2, which would inhibit the formation of fructose-2,6-bisphosphate.
O The rate of gluconeogenesis would be diminished, since PKA would be unable to inhibit the formation of fructose-2,6-
bisphosphate through phosphorylation of PFK2.
Transcribed Image Text:If the serine phosphorylated by Protein Kinase A (PKA) on phosphofructokinase-2 (PFK2) were mutated to an aspartate, how might this affect gluconeogenesis in the liver? O The rate of gluconeogenesis would be unchanged, since PKA would be unable to inhibit the formation of fructose-2,6- bisphosphate through phosphorylation of PFK2. O The rate of gluconeogenesis would increase, since PKA would phosphorylate an aspartate instead of a serine residue on PEK2, which would inhibit the formation of fructose-2,6-bisphosphate. O The rate of gluconeogenesis would increase, since PKA would phosphorylate an aspartate instead of a serine residue on PFK2, which would activate the formation of fructose-2,6-bisphosphate. O The rate of gluconeogenesis would be diminished, since PKA would phosphorylate an aspartate instead of a serine residue on PFK2, which would inhibit the formation of fructose-2,6-bisphosphate. O The rate of gluconeogenesis would be diminished, since PKA would be unable to inhibit the formation of fructose-2,6- bisphosphate through phosphorylation of PFK2.
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