Chemistry: An Introduction to General, Organic, and Biological Chemistry (13th Edition)
13th Edition
ISBN: 9780134421353
Author: Karen C. Timberlake
Publisher: PEARSON
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Chapter 16.5, Problem 16.46PP
The following graph shows the activity versus pH curves for pepsin, sucrase, and trypsin. Estimate the optimum pH for each.
16.46 Refer to the graph in problem 16.45 to determine if the reaction rate in each condition will be at the optimum rate or not.
- Trypsin, pH 5.0
- Sucrase, pH 5.0
- Pepsin, pH 4.0
- Trypsin, pH 8.0
- Pepsin, pH 2.0
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Answer question 16.46
40) Use the following information to answer the question below.
+100-
19.0
+80
+70-
+6.0
+50-
+4.0
+3.0-
+20-
+1.0
+2.0
+4.0
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-10
Concentration of reactants. inicremolar
Rate of an enzyme-catalyzed reaction as a function of varying reactant concentration, with the concentration
of enzyme constant
In the figure, why does the reaction rate plateau at higher reactant concentrations?
A) The rate of the reverse reaction increases at high reactant concentrations.
B) Feedback inhibition by product occurs at high reactant concentrations.
C) The reaction nears equilibrium at high reactant concentrations.
D) Most enzyme molecules are occupied by substrate at high reactant concentrations.
Rate of product formation
explain why the rate of reaction initially increases with temp?
Chapter 16 Solutions
Chemistry: An Introduction to General, Organic, and Biological Chemistry (13th Edition)
Ch. 16.1 - Classify each of the following proteins according...Ch. 16.1 - Prob. 16.2PPCh. 16.1 - Prob. 16.3PPCh. 16.1 - Prob. 16.4PPCh. 16.1 - Draw the structure for each of the following amino...Ch. 16.1 - Draw the structure for each of the following amino...Ch. 16.1 - Draw the strcture for each of the following amino...Ch. 16.1 - Prob. 16.8PPCh. 16.1 - Prob. 16.9PPCh. 16.1 - Prob. 16.10PP
Ch. 16.2 - Prob. 16.11PPCh. 16.2 - Prob. 16.12PPCh. 16.2 - Prob. 16.13PPCh. 16.2 - Prob. 16.14PPCh. 16.2 - Prob. 16.15PPCh. 16.2 - Prob. 16.16PPCh. 16.3 - Prob. 16.17PPCh. 16.3 - Prob. 16.18PPCh. 16.3 - Prob. 16.19PPCh. 16.3 - Prob. 16.20PPCh. 16.3 - What type of interaction would you expect between...Ch. 16.3 - What type of interaction would you expect between...Ch. 16.3 - Prob. 16.23PPCh. 16.3 - Prob. 16.24PPCh. 16.3 - Prob. 16.25PPCh. 16.3 - Prob. 16.26PPCh. 16.3 - Prob. 16.27PPCh. 16.3 - Indicate the changes in secondary and tertiary...Ch. 16.4 - Why do chemical reactions in the body require...Ch. 16.4 - Prob. 16.30PPCh. 16.4 - Prob. 16.31PPCh. 16.4 - Prob. 16.32PPCh. 16.4 - Prob. 16.33PPCh. 16.4 - Prob. 16.34PPCh. 16.4 - Prob. 16.35PPCh. 16.4 - 16.36 Match the terms (1) active site, (2)...Ch. 16.4 - Prob. 16.37PPCh. 16.4 - Prob. 16.38PPCh. 16.4 - Prob. 16.39PPCh. 16.4 - Prob. 16.40PPCh. 16.4 - For problems 16.39 to 16.42, see Chemistry Link to...Ch. 16.4 - Prob. 16.42PPCh. 16.5 - Trypsin, a peptidase that hydrolyzes polypeptides,...Ch. 16.5 - pepsin, a peptidase that hydrolyzes proteins,...Ch. 16.5 - The following graph shows the activity versus pH...Ch. 16.5 - The following graph shows the activity versus pH...Ch. 16.5 - Prob. 16.47PPCh. 16.5 - Prob. 16.48PPCh. 16.5 - Prob. 16.49PPCh. 16.5 - Prob. 16.50PPCh. 16.5 - What is the chemical formula for hydroxyurea?Ch. 16.5 - What is the molar mass of hydroxyurea?Ch. 16.5 - Prob. 16.53PPCh. 16.5 - Prob. 16.54PPCh. 16 - Prob. 16.55UTCCh. 16 - Prob. 16.56UTCCh. 16 - Prob. 16.57UTCCh. 16 - Prob. 16.58UTCCh. 16 - 16.59 Identify the amino acids and type of...Ch. 16 - What type of interaction would you expect between...Ch. 16 - Draw the condensed structural formula for...Ch. 16 - Draw the condensed structural formula for...Ch. 16 - Seed and vegetables are often deficient in one or...Ch. 16 - 16.64 Seeds and vegetables are often deficient in...Ch. 16 - Prob. 16.65APPCh. 16 - Prob. 16.66APPCh. 16 - Prob. 16.67APPCh. 16 - Prob. 16.68APPCh. 16 - Prob. 16.69APPCh. 16 - Why do enzymes function only under mild...Ch. 16 - Prob. 16.71APPCh. 16 - Prob. 16.72APPCh. 16 - Prob. 16.73APPCh. 16 - Prob. 16.74APPCh. 16 - Prob. 16.75APPCh. 16 - Prob. 16.76APPCh. 16 - Prob. 16.77APPCh. 16 - Prob. 16.78APPCh. 16 - If a blood test indicates a high level of LDH and...Ch. 16 - Prob. 16.80APPCh. 16 - Prob. 16.81CPCh. 16 - Prob. 16.82CP
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- When handling or storing solutions of enzymes, the pH is usually kept near 7.0. Explain why.arrow_forwardsac ve ha inhihi- The following graph shows the activity versus pH curves for pepsin, sucrase, and trypsin. Estimate the optimum pH for each. Maximum activity No activity Pepsin Sucrase Trypsin 01234 567 pH 8 9 10 11 12 16.46 Refer to the graph in problem 16.45 to determine if the reaction rate in each condition will be at the optimum rate or not. a. trypsin, pH 5.0 d. trypsin, pH 8.0 b. sucrase, pH 5.0 c. pepsin, pH 4.0 e. pepsin, pH 2.0arrow_forwardPlease explain why this anwser was wrong for question 1 and what the errors made were. If possible also please explain how you can get the correct anwser for this problem.arrow_forward
- A process that occurs in the human body is shown in the diagram (arrow's direction points to the direction of this hydrolysis reaction). What would happen if a temperature change -caused the shape of the enzyme's active site to be altered? + Active Site Dipeptide (Substrate) )-( Enzyme Enzyme-substrate Amino complex acids Dipeptide Breakdown ) - G The dipeptide would hydrolyze slower or not at all O The amino acids would combine slower or not at all The dipeptide would hydrolyze (break down) faster There will be no effect on the rate of this hydrolysis reaction The amino acids would combine faster + } Enzymearrow_forwardPlease don't provide handwritten solution .....arrow_forwardThe following grap shows the relationship between enzyme activity and both pH and temperature for two enzymes (A and B). Based on this graphical information What is the optimum pH for enzyme A? What is the optimum temperature for enzyme B? Which enzyme has the greater activity at a pH of 4? Which enzyme has the greater activity at a temperature of 37.8°C?arrow_forward
- The lock and key model and the induced fit model are two models of enzyme action explaining both the specificity and the catalytic activity of enzymes. Indicate whether each statement is part of the lock and key model, the induced fit model, or is common to both models. Lock and key model Induced fit model Common to both models Answer Bank The substrate binds to the enzyme at the active site, forming an enzyme-substrate complex. The substrate binds to the enzyme through noncovalent interactions. The enzyme conformation changes when it binds the substrate so that the active site fits the substrate. The enzyme active site has a rigid structure complementary to that of the substrate.arrow_forwardWhat do we mean when we say an enzyme is saturated with substrate? When an enzyme is saturated with substrate, how does adding more (a) substrate and (b) enzyme affect the rate of the reaction?arrow_forward10. Factor In the enzyme catalyzed reaction depicted above, which factor could be changed (increased) to produce the graph? (Assume an unlimited substrate supply and change in the factor) a. inhibitor concentration Ob. temperature Oc. pH Od. enzyme concentrationarrow_forward
- Juan performed the same chemical reaction twice. His data from the first at- tempt is indicated by the red line. His data from the second attempt is indicated by the blue line. Energy During a Chemical Reaction Energy A B reactants e.g. C6H12O6 + O₂ C without enzyme Juan added pressure. with enzyme Reaction coordinate What change did Juan most likely make to his reaction the second time he per- formed it? activation energy with enzyme D Juan added a catalyst. Juan increased the surface area of the reactants. Juan cooled his reactants. activation energy without enzyme overall energy released during reaction products CO,+H,Oarrow_forward3. Some medications permanently inactivate their target enzyme by forming a covalent bond to an amino acid in the enzyme's active site. Aspirin is one example of a pharmaceutical that uses this type of mechanism. So is penicillin. As you saw in the last chapter, the active portion of penicillin is the B-lactam ring. Penicillin forms a covalent bond to serine in the active site transpeptidase, an enzyme that is essential for forming the bacterial cell wall. Propose a mechanism for the inactivation of transpeptidase by penicillin and show the final product of the reaction. NH OH CH3 CH2 CH3 backbone penicillin serinearrow_forwardSubject- chemistryarrow_forward
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