Please don't provide handwritten solution 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 theliver?The rate of gluconeogenesis would increase, since PKA would phoshporylate anaspartate instead of a drine residue on PFK-2, which would activate theformation of fructose-2,6-bisphosphate.The rate of gluconeogenesis would be increase, since PKA would phosphorylatean aspartate instead of a serine residue on PFK-2, which would inhibit formationof fructose-2,6-bisphosphate.The rate of gluconeogenesis would be unchanged, since PKA would be unable toinhibit the formation of fructose-2,6-bisphosphate through phosphorylation ofPFK-2.The rate of gluconeogenesis would be diminished, since PKA wouldphosphorylate an aspartate instead of a serine residue on PFK-2, which wouldinhibit the formation of fructose-2,6-bisphosphate.The rate of gluconeogenesis would be diminished, since PKA would be unable toinhibit the formation of fructose-2.6-bisphosphate through phosphorylation ofPFK-2.

Glucose levels in the blood are maintained by glycolysis (catabolism) and gluconeogenesis…

Answered: If the serine phoshorylated by Protein…

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

Section: Chapter Questions

Problem 10P

See similar textbooks

Similar questions

Diisopropylphosphofluoridate (DIPF) inactivates chymotrypsin by covalently modifying serine 195. Which statement is true of DIPF's inhibitory mechanism? DIPF randomly modifies all serine residues on the protein, and if enough is added, the serine in the active site will eventually be modified. DIPF approaches serine 195 more closely than other substrates. DIPF looks like the substrate for chymotrypsin and binds in the active site as a competitive inhibitor. Serine 195 is in an environment that gives it a higher than normal reactivity with respect to DIPF.
TPCK and TLCK are irreversible inhibitors of serine proteases. One ofthese inhibits trypsin and the other chymotrypsin. Which is which? Explainyour reasoning. Suggest the effects of each of the following mutations on the physiologicalrole of chymotrypsinogen:(a) R15S(b) C1S(c) T147S
TLCK and TPCK both use Histadine residues in the active site as inhibitors of serine proteases. Why is TLCK specific for trypsin and TPCK is specific for chymotrypsin?
Will the amount of glycogen be higher or lower than normal or unchanged? Pyridoxal phosphate is covalently bonded to glycogen phosphorylase via a Schiff base to Lys 680. What effect would the mutation of Lys680Ala have on the breakdown of glycogen?(This notation means the following: K680 is the normal amino acid in this enzyme. It has been mutated to 680A.) Loss of the gene for the kinase that phosphorylates GSK3 on glycogen synthesis. Effect of the substrate analog below on glycogen synthesis.
You have isolated a new protease that cleaves peptide bonds on the carboxyl side of Asp and Glu. Based on the enzyme's inactivation by DIPF, you suspect that it may utilize a mechanism similar to chymotrypsin. The difference in specificity might be explained by the absence of the S1 binding pocket. replacement of serine 195 with a positively charged residue. presence of a positively charged residue in the S1 binding pocket. presence of a negatively charged residue in the S1 binding pocket.
At body temperature, L-aspartate in proteins race-mizes to D-aspartate at an appreciable rate. Most pro-teins in the body have a very low level of D-aspartate, if itcan be detected at all. Elastin, however, has a fairly highlevel of D-aspartate. Moreover, the amount of D-aspartateincreases in direct proportion to the age of the person fromwhom the sample was taken. Why do you suppose thatmost proteins have little if any D-aspartate, while elastinhas levels of D-aspartate that increase steadily with age?
Why Phenylmethylsulfonyl fluoride (PMSF, shown in Fig.) does not inhibit aspartate protease as potent as serine protease?
Describe the role of pH in regulating the interaction between mannose 6-phosphate and the M6P receptor. Why does a rise in endosomal pH lead to the secretion of newly synthesized lysosomal enzymes into the extracellular medium?
What would be the effect on the activity of phosphofructokinase of the mutation of Asp103 to the unusual amino acid shown below? Explain in terms of actual structures of the side chains of Asp and this unusual amino acid.
What is the logic behind high levels of arginine positivelyregulating N-acetylglutamate synthase?
How does the presence of the poorly hydrolyzable GTP analog GTP?S (in which an O atom on the terminal phosphate is replaced by an S atom) affect cAMP production by adenylate cyclase?
Considering the gluconeogenesis that may occur after removal of the amino group from amino acids, will malate be an intermediate in all such metabolic routes between amino acids and glucose? Explain. The phosphoenolpyruvate carboxykinase (PEPCK) gene is more actively transcribed when glucagon is present in blood. Putting the signal cascade responsible for that activation aside for the moment, will the reaction that PEPCK mediates be in zero or first order for that increased transcription to have a maximal affect on gluconeogenesis? Explain.

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS