You have discovered a ubiquitin (Lys48) ligase that is activated when human cells have high cyclic AMP. Which of the followingis the most logical and consistent with the role of cyclic AMP?O The ubiquitin ligase causes polyubiquitylation of glycogen synthase.O The ubiquitin ligase causes polyubiquitylation of the active catalytic PKA subunits.O The ubiquitin ligase causes polyubiquitylation of ATP.The ubiquitin ligase causes polyubiquitylation of CREB

polyubiquitination of a protein leads to degradation thereby maintains protein load in a cell.

Answered: You have discovered a ubiquitin (Lys48)…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter4: Cells

Section: Chapter Questions

Problem 1ITD

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The enzyme aspartate transcarbamoylase catalyzes an early step in pyrimidine biosynthesis. The two states of the multi-subunit enzyme are shown below. Note that the binding of the regulatory molecule CTP (cytosine triphosphate) causes the enzyme complex to be inactive. Is this situation an example of positive or negative regulation? Explain why the use of CTP as the regulatory molecule is logical givén the overall function of this particular enzyme. INACTIVE ENZYME: T STATE catalytic subunits regulatory subunits OFF 6 CTP ON ACTIVE ENZYME: R STATE
The graph displays the activities of wild-type and several mutated forms of subtilisin on a logarithmic scale. 5 The mutations are identified as: • The first letter is the one-letter abbreviation for the amino acid being altered. • The number identifies the position of the residue in the primary structure. The second letter is the one-letter abbreviation for the amino acid replacing the original one. • Uncat. refers to the estimated rate for the uncatalyzed reaction. Log ₁0k cat (S-¹) -5 -10 Wild type D32A S221A H64A İnti. S221A H64A D32A Uncat. How would the activity of a reaction catalyzed by a version of subtilisin with all three residues in the catalytic triad mutated compare to the activity of the uncatalyzed reaction? O It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster than the uncatalyzed reaction. It would have more activity, because the reaction catalyzed by the triple mutant is approximately three-fold faster…
In bacteria, isocitrate dehydrogenase is regulated by phosphorylation of a specific Ser residue in the enzyme active site. X-ray structures of the phosphorylated and the nonphosphorylated enzyme show no significant conformational differences. How does phosphorylation regulate isocitrate dehydrogenase activity? O The phosphoryl group sterically hinders the substrate. O The phosphorylation bears a negative charge, which repels the substrate. O The phosphoryl group attracts positively charged Ca2* cations, which block the active site on the enzyme. None of the above.
Trypsin uses a nearly identical mechanism as chymotrypsin (including the catalytic triad his57-ser195-asp102. beginning with the enzyme substrate complex draw the complete steps in the trypsin mechanism that occur to release the first product and create the acyl enzyme intermediate in the trypsin active site. The substrate for trypsin to be used is gly-lys-gly-ala
The enzyme mutase which is important for the synthetic of tyrosine and phenylalanine in saccharomyces cerevisiae has been studied as an example of an allosteric enzyme. Tyrosine acts as a negative effector for this enzyme. What effects would you see on the action of the enzyme were you to increase the concentration of tyrosine? The chorismate mutase would shift to its R conformation The curve showing the kinetics or chorismate mutase would shift to the right The curve showing the kinetics of chorismate mutase would shift to the left The chorismate mutase would become saturated more rapidly
From the complete oxidation of glucose (glucose → 6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation?
#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)
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…
From the complete oxidation of glucose (glucose 6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation? 灣
UDP-glucose pyrophosphorylase catalyzes the removal of a pyrophosphate group from UTP as it synthesizes UDP-glucose. Why is this necessary, from a biochemical perspective? Both of the phosphate groups from UTP are needed to form UDP-glucose. There is no particular reason: wasteful reactions just happen sometimes. The pyrophosphate (after hydrolysis) is required to free up more phosphate for the synthesis of ATP by oxidative phosphorylation. The subsequent hydrolysis of pyrophosphate is a highly exergonic reaction, which pulls the equilibrium over towards UDP-glucose. Pyrophosphate is an allosteric activator of glycogen synthase, so this helps glycogen synthesis to proceed at a faster rate.
Glutamine affects the regulatory system for E. coli glutamine synthetase so as to promote the adenylylation of glutamine synthetase and inhibit the deadenylylation. Why do these effects make good metabolic sense?
Aspartate transcarbamoylase, which is necessary for CTP production, is an essential enzyme for the human body. In the below graph, which line represents the rate of the reaction catalyzes by Aspartate transcarbamoylase? Explain.

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