Biochemistry, The Molecular Basis of Life, 6th Edition
6th Edition
ISBN: 9780190259204
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Chapter 15, Problem 8RQ
Summary Introduction
To review:
Definition of the following terminologies:
(a) Albinism
(b) Maple syrup urine disease
(c) Alkaptonuria
(d) Methylmalonic acidemia
(e) Phenylketonuria
Introduction:
The catabolism of various amino acids requires enzymesand is necessary for the proper functioning of different biological processes. The various end products released after catabolism of amino acids are acetyl CoA (coenzyme A), pyruvate, acetoacetyl CoA, and several intermediates of the citric acid cycle such as alpha-ketoglutarate, succinyl CoA, and oxaloacetate. Enzymes are function optimally in healthy individuals. The disorders associated with amino acid
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what is a protein that contains a b-sheet and how does the secondary structure contributes to the overall function of the protein.
Chapter 15 Solutions
Biochemistry, The Molecular Basis of Life, 6th Edition
Ch. 15 - Prob. 1QCh. 15 - Prob. 2QCh. 15 - Prob. 5QCh. 15 - Prob. 6QCh. 15 - Prob. 7QCh. 15 - Prob. 1RQCh. 15 - Prob. 2RQCh. 15 - Prob. 3RQCh. 15 - Prob. 4RQCh. 15 - Prob. 5RQ
Ch. 15 - Prob. 6RQCh. 15 - Prob. 7RQCh. 15 - Prob. 8RQCh. 15 - Prob. 9RQCh. 15 - Prob. 10RQCh. 15 - Prob. 11RQCh. 15 - Prob. 12RQCh. 15 - Prob. 13RQCh. 15 - Prob. 14RQCh. 15 - Prob. 15RQCh. 15 - Prob. 16RQCh. 15 - Prob. 17RQCh. 15 - Prob. 18RQCh. 15 - Prob. 19RQCh. 15 - Prob. 20RQCh. 15 - Prob. 21RQCh. 15 - Prob. 22RQCh. 15 - Prob. 23RQCh. 15 - Prob. 24RQCh. 15 - Prob. 25RQCh. 15 - Prob. 26RQCh. 15 - Prob. 27RQCh. 15 - Prob. 28RQCh. 15 - Prob. 29RQCh. 15 - Prob. 30RQCh. 15 - Prob. 31RQCh. 15 - Prob. 32RQCh. 15 - Prob. 33RQCh. 15 - Prob. 34RQCh. 15 - Prob. 35RQCh. 15 - Prob. 36RQCh. 15 - Prob. 37RQCh. 15 - Prob. 38RQCh. 15 - Prob. 39RQCh. 15 - Prob. 40RQCh. 15 - Prob. 41RQCh. 15 - Prob. 42RQCh. 15 - Prob. 43RQCh. 15 - Prob. 44RQCh. 15 - Prob. 45FBCh. 15 - Prob. 46FBCh. 15 - Prob. 47FBCh. 15 - Prob. 48FBCh. 15 - Prob. 49FBCh. 15 - Prob. 50FBCh. 15 - Prob. 51FBCh. 15 - Prob. 52FBCh. 15 - Prob. 53FBCh. 15 - Prob. 54FBCh. 15 - Prob. 55SACh. 15 - Prob. 56SACh. 15 - Prob. 57SACh. 15 - Prob. 58SACh. 15 - Prob. 59SACh. 15 - Prob. 60TQCh. 15 - Prob. 61TQCh. 15 - Prob. 62TQCh. 15 - Prob. 63TQCh. 15 - Prob. 64TQCh. 15 - Prob. 65TQCh. 15 - Prob. 66TQCh. 15 - Prob. 67TQCh. 15 - Prob. 68TQCh. 15 - Prob. 69TQCh. 15 - Prob. 71TQCh. 15 - Prob. 72TQCh. 15 - Prob. 73TQCh. 15 - Prob. 74TQ
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- draw and annotate a b-sheet and lable the hydrogen bonding. what is an example that contains the b-sheet and how the secondary structure contributes to the overall function of your example protein.arrow_forwardFour distinct classes of interactions (inter and intramolecular forces) contribute to a protein's tertiary and quaternary structures. Name the interaction then describe the amino acids that can form this type of interaction. Draw and annotate a diagram of the interaction between two amino acids.arrow_forwardExamine the metabolic pathway. The enzymes that catalyze each step are identified as "e" with a numeric subscript. e₁ e3 e4 A B с 1° B' 02 e5 e6 e7 E F Which enzymes catalyze irreversible reactions? ப e ez ☐ ez e4 ☐ ப es 26 5 e7 Which of the enzymes is likely to be the allosteric enzyme that controls the synthesis of G? €2 ез e4 es 26 5 e7arrow_forward
- An allosteric enzyme that follows the concerted model has an allosteric coefficient (T/R) of 300 in the absence of substrate. Suppose that a mutation reversed the ratio. Select the effects this mutation will have on the relationship between the rate of the reaction (V) and substrate concentration, [S]. ㅁㅁㅁ The enzyme would likely follow Michaelis-Menten kinetics. The plot of V versus [S] would be sigmoidal. The enzyme would mostly be in the T form. The plot of V versus [S] would be hyperbolic. The enzyme would be more active.arrow_forwardPenicillin is hydrolyzed and thereby rendered inactive by penicillinase (also known as ẞ-lactamase), an enzyme present in some penicillin-resistant bacteria. The mass of this enzyme in Staphylococcus aureus is 29.6 kDa. The amount of penicillin hydrolyzed in 1 minute in a 10.0 mL. solution containing 1.00 x 10 g of purified penicillinase was measured as a function of the concentration of penicillin. Assume that the concentration of penicillin does not change appreciably during the assay. Plots of V versus [S] and 1/V versus 1/[S] for these data are shown. Vo (* 10 M minute"¹) 7.0 6.0 5.0 4.0 3.0 20 1.0 0.0 о 10 20 30 1/Vo (* 10 M1 minute) 20 103 90 BO 70 50 [S] (* 100 M) 40 50 60 y=762x+1.46 × 10" [Penicillin] (M) Amount hydrolyzed (uM) 1 0.11 3 0.25 5 0.34 10 0.45 30 0.58 50 0.61arrow_forwardConsider the four graphs shown. In each graph, the solid blue curve represents the unmodified allosteric enzyme and the dashed green curve represents the enzyme in the presence of the effector. Identify which graphs correctly illustrate the effect of a negative modifier (allosteric inhibitor) and a positive modifier (allosteric activator) on the velocity curve of an allosteric enzyme. Place the correct graph in the set of axes for each type of modifier. Negative modifier Reaction velocity - Positive modifier Substrate concentration - Reaction velocity →→→→ Substrate concentration Answer Bankarrow_forward
- Consider the reaction: phosphoglucoisomerase Glucose 6-phosphate: glucose 1-phosphate After reactant and product were mixed and allowed to reach at 25 °C, the concentration of each compound at equilibrium was measured: [Glucose 1-phosphate] = 0.01 M [Glucose 6-phosphate] = 0.19 M Calculate Keq and AG°'. Код .0526 Incorrect Answer 7.30 AG°' kJ mol-1 Incorrect Answerarrow_forwardClassify each phrase as describing kinases, phosphatases, neither, or both. Kinases Phosphatases Neither Both Answer Bank transfer phosphoryl groups to acidic amino acids in eukaryotes may use ATP as a phosphoryl group donor remove phosphoryl groups from proteins catalyze reactions that are the reverse of dephosphorylation reactions regulate the activity of other proteins catalyze phosphorylation reactions PKA as an example turn off signaling pathways triggered by kinasesarrow_forwardConsider the reaction. kp S P kg What effects are produced by an enzyme on the general reaction? AG for the reaction increases. The rate constant for the reverse reaction (kr) increases. The reaction equilibrium is shifted toward the products. The concentration of the reactants is increased. The activation energy for the reaction is lowered. The formation of the transition state is promoted.arrow_forward
- The graph displays the activities of wild-type and several mutated forms of subtilisin on a logarithmic scale. 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. Log₁(S-1) Wild type S221A H64A -5 D32A S221A H64A D32A -10 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? It would have more activity, because the reaction catalyzed by the triple mutant is approximately three-fold faster than the uncatalyzed reaction. It would have less activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold slower than the…arrow_forwardB Substrate Product AL Product Substrate Reaction progress- Reaction progress- omplete the passage describing the two reactions. In reaction A, the stability of the substrate is (AG) of the reaction is positive, Incorrect Answer greater than the stability of the product. The free-energy change Incorrect Answer so the reaction is considered In reaction B, the stability of the substrate is (AG) of the reaction is less than Incorrect Answer endergonic and Incorrect Answer not spontaneous. Incorrect Answer the stability of the product. The free-energy change negative, so the reaction is considered Incorrect Answer exergonic and spontaneous. Incorrect Answer Incorrect Answerarrow_forwardMatch the descriptions and compounds with the terms competitive, uncompetitive, and noncompetitive inhibition. Competitive inhibition Uncompetitive inhibition Noncompetitive inhibition Answer Bank inhibitor binds to the enzyme-substrate complex only Vmax remains the same but Ky increases inhibitor and substrate can bind simultaneously lowers Vmax and KM doxycycline sulfanilamide KM remains unchanged, but Vis lower prevents substrate from binding to the active site Rounduparrow_forward
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