Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
8th Edition
ISBN: 9780134015187
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
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Chapter 25, Problem 25.56GP
Interpretation Introduction
Interpretation:
The number of ATPs that are consumed a tetra peptide has to be determined.
Concept Introduction:
Amino acids:
The organic compounds which has nitro group and carbonyl group as a
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Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere
on the protein (phosphorylation). The basic reaction is:
E + ATP2 Ep + ADP
Po
SERINE
PHOSPHO SERINC
(Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues
on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium
between inactive and active forms conformations of the enzyme:
[Eactive]
[Einactive]
Einactive 2 Eactive; K*
The same basic equilibrium must exist for the phosphorylated protein:
[Ep,active]
[Ep,inactive]
EP,inactive 2 Ep,active; Kp =
(a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why?
(b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate
(e.g. the reactant whose chemistry it catalyzes)? Why or why not?
Draw the structure of the a-keto acid formed by removal of the amino group during the catabolism of leucine.
Note: Reference the Naturally-occurring amino acids table for additional information.
Click and drag to start drawing a
structure.
x
A mutation has occurred that results in phosphofructokinase not being able to bind ATP in its allosteric site. What impact will this mutation have on the production of ATP in the cell?
Select one:
a. If no ATP can bind to the allosteric site, then phosphofructokinase will not be able to add the phosphate to fructose-6-phosphate to make fructose-1,6-bisphosphate and glycolysis will not work. So no pyruvate, not cellular respiration.
b. If ATP cannot bind to the allosteric site, phosphofructokinase will not be activated to make more ATP by substrate-level phosphorylation.
c. No impact on the production but will not be able to effectively shut off over production of ATP with feedback inhibition.
Chapter 25 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
Ch. 25.2 - Prob. 25.1PCh. 25.2 - Prob. 25.2KCPCh. 25.3 - Prob. 25.3PCh. 25.3 - Prob. 25.4PCh. 25.3 - Prob. 25.5PCh. 25.3 - Prob. 25.6PCh. 25.4 - Prob. 25.1CIAPCh. 25.4 - Prob. 25.2CIAPCh. 25.4 - Prob. 25.3CIAPCh. 25.4 - Prob. 25.7P
Ch. 25.4 - Prob. 25.8KCPCh. 25.6 - Prob. 25.9PCh. 25.6 - Prob. 25.10KCPCh. 25.6 - What is meant by a conditional amino acid?Ch. 25.6 - Prob. 25.5CIAPCh. 25.6 - Prob. 25.6CIAPCh. 25 - In the diagram shown here, fill in the sources for...Ch. 25 - Prob. 25.12UKCCh. 25 - Prob. 25.13UKCCh. 25 - Prob. 25.14UKCCh. 25 - Prob. 25.15UKCCh. 25 - Prob. 25.16UKCCh. 25 - Prob. 25.17APCh. 25 - Prob. 25.18APCh. 25 - Prob. 25.19APCh. 25 - Prob. 25.20APCh. 25 - Prob. 25.21APCh. 25 - Prob. 25.22APCh. 25 - What is the structure of the -keto acid formed...Ch. 25 - Prob. 25.24APCh. 25 - In general, how does oxidative deamination differ...Ch. 25 - Prob. 25.26APCh. 25 - Prob. 25.27APCh. 25 - Prob. 25.28APCh. 25 - Prob. 25.29APCh. 25 - Prob. 25.30APCh. 25 - Prob. 25.31APCh. 25 - Prob. 25.32APCh. 25 - Prob. 25.33APCh. 25 - Prob. 25.34APCh. 25 - How do essential and nonessential amino acids...Ch. 25 - Prob. 25.36APCh. 25 - Prob. 25.37APCh. 25 - How is tyrosine biosynthesized in the body? What...Ch. 25 - Prob. 25.39APCh. 25 - Prob. 25.40APCh. 25 - Prob. 25.41APCh. 25 - What energy source is used in the formation of...Ch. 25 - Write the equation for the transamination reaction...Ch. 25 - Prob. 25.44CPCh. 25 - Prob. 25.45CPCh. 25 - Prob. 25.46CPCh. 25 - Prob. 25.47CPCh. 25 - Prob. 25.48CPCh. 25 - Prob. 25.49CPCh. 25 - Prob. 25.50CPCh. 25 - Prob. 25.51CPCh. 25 - Prob. 25.52CPCh. 25 - Why might it be a bad idea to take large...Ch. 25 - Prob. 25.54GPCh. 25 - Prob. 25.55GPCh. 25 - Prob. 25.56GP
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Describe the catabolism of a the amino acid serine. Start with serine and end with ATP. Give the details of every step.arrow_forwardUse the following information to answer the next question. The DNA strand shown below is thought to contain the genetic code for part of an enzyme B-galactosidase which is involved in lactose metabolism. (Read the DNA beginning at the left.) -A-T-A-T-G-G-G-G-C-A-T-G The second amino acid coded from the section of DNA for B-galactosidase is Select one: a. thymine b. tryptophan c. serine d. threoninearrow_forwardThe hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 umol of pyrophosphate in 15 minutes. The purified enzyme has a Vnax of 2800 U per milligram of enzyme. When (S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second? Vnas umol-s. mg-! max If each enzyme subunit has one active site, how many micromoles of active sites, or (E]r, are there in 1 mg of enzyme? (Er= umol · mg-!arrow_forward
- Draw the formula of each of the following: a. Aspartic acid-histidine-tryptophan b. Glycine-cysteine-tyrosine with the charges that exist in cell fluid.arrow_forwardSome enzymes can be regulated by covalent modification, in which a group is covalently bonded to an amino acid side chain. Phosphorylation of side chains is a common regulatory covalent modification. In this essay, you will explore phosphorylation of side chains. Compare and contrast the types of interactions a free alcohol side chain such as serine could make with that of a phosphorylated alcohol such as phosphoserine (pSer). Could this modification affect the 3D structure of the protein? How? Imagine you are trying to separate a protein containing an unphosphorylated S residue from the same protein containing a pSer residue. Discuss how you could use ion-exchange chromatography to separate these two proteinsarrow_forwardThe structures of the amino acids leucine and isoleucine are shown: H 0 OH H CH, CH H₂C CH₂ Leucine CH H₂C OH CH₂ CH₂ Isoleucine a. Explain how the structure of amino acids determine the function. b. A mutation occurred in DNA of a globular enzyme. If the leucine amino acids were found within the active site of the enzyme, describe the effect this change is likely to have on enzymatic function. c. If a mutation in the DNA of a globular enzyme changed all of the leucine amino acids to isoleucine, predict how the relative position of the amino acid in the tertiary structure of the protein would be affected when the protein is placed in an aqueous solution. d. Justify your prediction by providing evidence that supports your claim.arrow_forward
- The image below shows an amino acid at physiological pH. Answer the following questions about this amino acid. H | // - c H3N* | CH2 CH2 | H2N a. How many carbons are in this amino acid's side chain? Entry Format: please type your answer as a number. 3 b. Is the side chain of this amino acid ionized at physiological pH? Entry Format: Please type the word yes or no without any capitalization. yes c. At physiological pH, amino acids have two ionic charges, one positively charged group and one negatively charged group. What is the term for this sort of molecule? Entry Format: Please type your response with all lowercase letters.arrow_forwardUsing the figure below, determine the metabolic intermediate(s) directly produced from the carbon atoms of each of the following amino acids. Check all that apply for each part. alanine, cysteine, isoleucine, leucine, Part 1 of 2 Valine leucine, lysine, glycine, serine, pyruvate threonine, tryptophan threonine, tryptophan phenylalanine, tryptophan, tyrosine acetyl CoA acetoacetyl CoA (CH,COCH,COSCA) asparagine, aspartic acid oxaloacetate citrate malate isocitrate Citric acid cycle phenylalanine, tyrosine fumarate Part 2 of 2 Asparagine fumarate acetoacetyl CoA pyruvate oxaloacetate succinyl CoA a-ketoglutarate acetyl CoA None of the above fumarate acetoacetyl CoA pyruvate oxaloacetate succinyl CoA a-ketoglutarate acetyl CoA None of the above a-ketoglutarate arginine, glutamic acid, glutamine, histidine, proline K succinate succinyl CoA isoleucine, methionine, threonine, valinearrow_forwardUsing your best guess, what percentage of the protein is alpha helices? What about beta sheets? Loops? The protein this would be for is branched-chain alpha-keto acid dehydrogenase.arrow_forward
- Glutamate, a 5-carbon amino acid, is the precursor of three other amino acids that contain a 5-carbon chain. Identify these amino acids.arrow_forwardDraw the structure of the α-keto acid formed by the transamination of each amino acid: (a) tyrosine; (b) asparagine.arrow_forwardPLP is a cofactor for a number of enzymes involved in amino acid metabolism. Give an example of reaction in which PLP participates in cleavage of the a, b, and c bonds of an amino acid, as diagrammed in shown Fig.arrow_forward
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