Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Textbook Question
Chapter 15, Problem 44RE
MATHEMATICAL The standard free-energy change for the reaction
is
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61. MATHEMATICAL For the following aspartase reaction (see Ques-
tion 28) in the presence of the inhibitor hydroxymethylaspar-
tate, determine K and whether the inhibition is competitive or
noncompetitive.
[S]
(molarity)
V, No Inhibitor
(arbitrary units)
V, Inhibitor Present
(same arbitrary units)
:21×10¹01 0.026 TOIV 0.0109 9
5 X 10
0.092
0.040
0.086
0.120
10-3
IPO?
2.5 10-³
5×10 211 0.150 09M
ein
5 X 10-3
0.165
20 mys
0.142
Initial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.
ENZYME KINETICS ANALYSIS
of 6
Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess
causes gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student
researcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO
which uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the
Lineweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table
2 and paste a copy of your Lineweaver-Burk plot. submit the picture of your output in PNG or JPG format.
Table 1. Enzyme Kinetic Data
Velocity, mM/s
[S], mM
Хan
Kmp
Cha
0.492
0.0678
0.0351
0.0615
0.211
0.0531
0.0261
0.0451
0.087
0.0298
0.0157
0.0211
0.048
0.0195
0.0091
0.0142
0.029
0.0127
0.0067
0.0081
Table 2. Enzyme Kinetic Parameters
Xanthine
Kaempferol
Chlorogenic acid
Parameters
Vmax
Км
Type of Inhibition
Mode of Binding
NA
NA
Lineweaver-Burk Plot
Chapter 15 Solutions
Biochemistry
Ch. 15 - RECALL Is there a connection between the...Ch. 15 - REFLECT AND APPLY What do the following indicators...Ch. 15 - REFLECT AND APPLY Consider the reaction...Ch. 15 - RECALL What conditions are necessary for the...Ch. 15 - REFLECT AND APPLY Why is it important that energy...Ch. 15 - RECALL Why is it necessary to define a modified...Ch. 15 - RECALL Which of the following statements is (are)...Ch. 15 - RECALL How can you tell if the standard Gibbs free...Ch. 15 - RECALL Can the thermodynamic property G be used to...Ch. 15 - MATHEMATICAL Calculate G for the following values...
Ch. 15 - Prob. 11RECh. 15 - MATHEMATICAL Consider the reaction AB+C, where...Ch. 15 - Prob. 13RECh. 15 - MATHEMATICAL The G for the reaction Citrate ...Ch. 15 - MATHEMATICAL If a reaction can be written AB, and...Ch. 15 - Prob. 16RECh. 15 - Prob. 17RECh. 15 - Prob. 18RECh. 15 - RECALL Organize the following words into two...Ch. 15 - Prob. 20RECh. 15 - REFLECT AND APPLY Would you expect the production...Ch. 15 - Prob. 22RECh. 15 - REFLECT AND APPLY Adult humans synthesize large...Ch. 15 - RECALL Identify the molecules oxidized and reduced...Ch. 15 - RECALL For each of the reactions in Question 24,...Ch. 15 - Prob. 26RECh. 15 - RECALL What is the structural difference between...Ch. 15 - RECALL How does the difference between NADH and...Ch. 15 - RECALL Which coenzyme is a reactant in the...Ch. 15 - Prob. 30RECh. 15 - Prob. 31RECh. 15 - Prob. 32RECh. 15 - REFLECT AND APPLY The following half reactions...Ch. 15 - Prob. 34RECh. 15 - REFLECT AND APPLY There is a reaction in...Ch. 15 - REFLECT AND APPLY There is a reaction in which...Ch. 15 - Prob. 37RECh. 15 - Prob. 38RECh. 15 - Prob. 39RECh. 15 - Prob. 40RECh. 15 - MATHEMATICAL Using the data in Table 15.1,...Ch. 15 - Prob. 42RECh. 15 - Prob. 43RECh. 15 - MATHEMATICAL The standard free-energy change for...Ch. 15 - Prob. 45RECh. 15 - Prob. 46RECh. 15 - Prob. 47RECh. 15 - REFLECT AND APPLY Would you expect an increase or...Ch. 15 - REFLECT AND APPLY Explain and show why...Ch. 15 - Prob. 50RECh. 15 - Prob. 51RECh. 15 - Prob. 52RECh. 15 - Prob. 53RECh. 15 - REFLECT AND APPLY Why are thioesters considered...Ch. 15 - Prob. 55RECh. 15 - REFLECT AND APPLY This is a conjectural question:...
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- MATHEMATICAL For an enzyme that displays MichaelisMenten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? (a) [S]=KM (b) [S]=0.5KM (c) [S]=0.1KM (d) [S]=2KM (e) [S]=10KMarrow_forwardMATHEMATICAL If a reaction can be written AB, and the G is 20kJmol1, what would the substrate/product ratio have to be for the reaction to be thermodynamically favorable?arrow_forwardMATHEMATICAL Consider the reaction AB+C, where G=0.00. (a) What is the value of G (not G) when the initial concentrations of A, B, and C are 1 M, 103M,and106M? (b) Try the same calculations for the reaction D+EF, for the same relative order of concentrations. (c) Try the same calculations for the reaction GH, if the concentrations are 1Mand103M for G and H, respectively.arrow_forward
- MATHEMATICAL Calculate the ATP yield for the complete oxidation of one molecule of palmitic acid (16 carbons). How does this figure differ from that obtained for stearic acid (18 carbons)?arrow_forwardMATHEMATICAL For the Vmax obtained in Question 26, calculate the turnover number (catalytic rate constant) assuming that 131024mol of enzyme were used.arrow_forwardMATHEMATICAL The G for the reaction Citrate Isocitrare is +6.64kJmol1=+1.59kcalmol1. The G for the reaction Isocitrate -Ketoglutrate is 267kJmol1=63.9kcalmol1. What is the G for the conversion of citrate to - ketoglutarate? Is that reaction exergonic or endergonic, and why?arrow_forward
- MATHEMATICAL Using the information in Table 20.2, calculate G for the following reaction: 2Cytaa3[oxidized;Fe(III)]+2Cytb[reduced;Fe(II)]2Cytaa3[reduced;Fe(II)]+2Cytb[oxidized;Fe(III)]arrow_forwardREFLECT AND APPLY Two biochemistry students are about to use mitochondria isolated from rat liver for an experiment on oxidative phosphorylation. The directions for the experiment specify addition of purified cytochrome c from any source to the reaction mixture. Why is the added cytochrome c needed? Why does the source not have to be the same as that of the mitochondria?arrow_forwardMATHEMATICAL Which is more favorable energetically, the oxidation of succinate to fumarate by NAD+ or by FAD? Give the reason for your answer.arrow_forward
- REFLECT AND APPLY In metabolism, glucose-6-phosphate (G6P) can be used for glycogen synthesis or for glycolysis, among other fates. What does it cost, in terms of ATP equivalents, to store G6P as glycogen, rather than to use it for energy in glycolysis? Hint: The branched structure of glycogen leads to 90% of glucose residues being released as glucose-1-phosphate and 10% as glucose.arrow_forwardREFLECT AND APPLY The enzyme lactate dehydrogenase catalyzes the reaction Pyruvate+NADH+H+lactate+NAD+ NADH absorbs light at 340 nm in the near-ultraviolet region of the electromagnetic spectrum, but NAD1 does not. Suggest an experimental method for following the rate of this reaction, assuming that you have available a spectrophotometer capable of measuring light at this wavelength.arrow_forwardREFLECT AND APPLY The malate-aspartate shuttle yields about 2.5 moles of ATP for each mole of cytosolic NADH. Why does nature use the glycerol-phosphate shuttle, which yields only about 1.5 moles of ATP?arrow_forward
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