If the serine phoshorylated by Protein Kinase A (PKA) on phosphofructokinase-2 (PFK-2) were mutated to an aspartate, how might this affect gluconeogenesis in the liver? The rate of gluconeogenesis would increase, since PKA would phoshporylate an aspartate instead of a drine residue on PFK-2, which would activate the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be increase, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be unchanged, since PKA would be unable to inhibit the formation of fructose-2,6-bisphosphate through phosphorylation of PFK-2. The rate of gluconeogenesis would be diminished, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be diminished, since PKA would be unable to inhibit the formation of fructose-2.6-bisphosphate through phosphorylation of PFK-2.

Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter26: Synthesis And Degradation Of Nucleotides
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If the serine phoshorylated by Protein Kinase A (PKA) on phosphofructokinase-2
(PFK-2) were mutated to an aspartate, how might this affect gluconeogenesis in the
liver?
The rate of gluconeogenesis would increase, since PKA would phoshporylate an
aspartate instead of a drine residue on PFK-2, which would activate the
formation of fructose-2,6-bisphosphate.
The rate of gluconeogenesis would be increase, since PKA would phosphorylate
an aspartate instead of a serine residue on PFK-2, which would inhibit formation
of fructose-2,6-bisphosphate.
The rate of gluconeogenesis would be unchanged, since PKA would be unable to
inhibit the formation of fructose-2,6-bisphosphate through phosphorylation of
PFK-2.
The rate of gluconeogenesis would be diminished, since PKA would
phosphorylate an aspartate instead of a serine residue on PFK-2, which would
inhibit the formation of fructose-2,6-bisphosphate.
The rate of gluconeogenesis would be diminished, since PKA would be unable to
inhibit the formation of fructose-2.6-bisphosphate through phosphorylation of
PFK-2.
Transcribed Image Text:If the serine phoshorylated by Protein Kinase A (PKA) on phosphofructokinase-2 (PFK-2) were mutated to an aspartate, how might this affect gluconeogenesis in the liver? The rate of gluconeogenesis would increase, since PKA would phoshporylate an aspartate instead of a drine residue on PFK-2, which would activate the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be increase, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be unchanged, since PKA would be unable to inhibit the formation of fructose-2,6-bisphosphate through phosphorylation of PFK-2. The rate of gluconeogenesis would be diminished, since PKA would phosphorylate an aspartate instead of a serine residue on PFK-2, which would inhibit the formation of fructose-2,6-bisphosphate. The rate of gluconeogenesis would be diminished, since PKA would be unable to inhibit the formation of fructose-2.6-bisphosphate through phosphorylation of PFK-2.
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