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)…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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serine proteases act via a two-step catalytic mechanism. However, as a critical scientist, you may want to see data that supports this claim. One experiment that can provide such evidence is called a 'pre-steady state' kinetics experiment using the chromogenic substrate, N-acetyl- phenylalanine p-nitrophenyl ester. As shown below when this substrate is cleaved, the p-nitrophenylate is a yellow product whose absorbance can be measured in real time using a spectrophotometer. When the chromogenic substrate is rapidly mixed together with a limiting amount of protease enzyme, the accumulation of product is measured right away on fast (millisecond) timescales. In this experiment, one observes two distinct phases of the reaction as shown in the plot below. Based upon what you know about the mechanism of serine proteases, provide a mechanistic interpretation for the observation of these two phases of the reaction. + H₂O N-Acetyl-L-phenylalanine p-nitrophenyl ester p-Nitrophenolate Absorbance…
PFK-1 is actually a tetramer with four identical active sites that produced fructose 1,6-bisphosphate. There are also allosteric sites for citrate and ATP/ADP on each subunit as well which influence how well the active sites are binding substrates or producing product. The arginine at position 48 on each PFK-1 subunit normally forms a salt bridge with a negatively charged oxygen on phosphate in the catalytic interface of PFK-1. Speculate on how the R48C mutation might change this function.
Which of the following statements about ribozyme catalytic residues is INCORRECT? General acid catalysis requires the standarde nucleotide exchangeable proton acidities (represented by pKa values). Ribozymes work by lowering the AG‡ through transition state stabilization without changing the overall AG of the reaction. Some ribozymes cleave phosphodiester bonds, and like proteases, can be autocatalytic. There are fewer known classes of mammalian ribozymes than mammalian enzyles.
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?
Consider an enzyme that catalyzes the reaction S2 P, by the following simple reaction mechanism: k, E + S 2 E•S →E kcat + P Suppose the enzyme acquires a mutation that causes k1 to be 10-times smaller than for the wild-type (non-mutant) enzyme. Suppose you measure the initial reaction rate (vo) at several different [S] for the mutant and the wild-type enzymes. Under what conditions would the mutation have a greater effect on the reaction rate (vo) of the mutant enzyme compared to the wild-type enzyme - at very low [S], or at very high [S]? Explain briefly how you decided.
Cyclic AMP (CAMP) is an important signaling molecule in cells. The synthesis and degradation of CAMP is diagrammed in the following figure: ATP ©2017 Pearson Education, Inc. 12pt Adenylyl cyclase Edit View Insert Format Tools Table Paragraph Pyrophosphate 3'c- P-P₁ 5'C BI Both caffeine (coffee, cola) and theophylline inhibit the enzyme phosphodiesterase that converts CAMP to AMP, allowing cAMP levels to temporarily remain high. Briefly discuss the possible effect of these drugs on the second messenger action of CAMP. What might the effect of caffeine of theophylline be on a signaling pathway? CAMP UA Phosphodiesterase T² H₂O AMP ⠀
the structures of chymotrypsin and other serine proteases revealed that the active sites of these enzymes shared a particular sterochemical arrangement of residues crucial to their activity. This came to be known as the catalytic triad, as it consisted of the oponyomous serine (Ser) residue, along with a histidine (His) and an aspartate (Asp) residue. Which of the following would result in the greatest decrease in function of the catalytic triad found in serine proteases? O Mutation to Ser, Cys, Asp O Mutation to Ser, His, Asp O Mutation to Cys, His, Asp O Mutation to Ser, His, Glu
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?
Suppose that an aspartic acid (aspartate) residue in the active site of an enzyme was mutated to alanine. As expected, the alanine mutant was inactive, suggesting that the aspartic acid residue was critical to the catalytic mechanism. Which mutation is most likely to restore wild-type level of activity to the alanine mutant? O A to Y A to M A to K A to E A to L
Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acety/A-ase Acetate - A-ase Deacetylase A-ase Protease & C-ase B-ase ABCD What is the mechanism of regulation of B-ase? Positive allostery Reversible Covalent modification Isoenzymes Proteolytic Activation Feedback Inhibition 1
In class, I mentioned that fructose is metabolized differently in the liver compared to glucose. Refer to the figure shown below to calculate the number ofATPs you would expect from the metabolism of fructose in the liver. Show your work! Fructokinase Fructose Fructose-1-P АТР ADP Aldolase B Dihydroxy- acetone phosphate Glyceraldehyde АТР Triose kinase Triose phosphate isomerase ADP 4 - Glyceraldehyde-3-P Glycolysis Руruvate Acetyl-CoA Fatty acids and triglycerides
ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate using adenosine diphosphate and inorganic phosphate. Which of the following are true for the protein, ATP synthase? Select all apply A mutation of Asp61 to glutamic acid would have less of a deleterious effect on its ability to synthesize ATP than a mutation of Asp61 to alanine A mutation of Asp61 to alanine would have less of a deleterious effect on its ability to synthesize ATP than a mutation of Asp61 to glutamic acid The F1 subunit is primarily responsible for translocating H+ ions across the inner mitochondrial membrane during ATP synthesis The FO subunit is primarily responsible for translocating H+ ions across the inner mitochondrial membrane during ATP synthesis

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