Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 20, Problem 50RE
MATHEMATICAL The free-energy change
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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
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
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.
Chapter 20 Solutions
Biochemistry
Ch. 20 - RECALL Briefly summarize the steps in the electron...Ch. 20 - RECALL Are electron transport and oxidative...Ch. 20 - Prob. 3RECh. 20 - REFLECT AND APPLY Show how the reactions of the...Ch. 20 - REFLECT AND APPLY How does mitochondrial structure...Ch. 20 - Prob. 6RECh. 20 - Prob. 7RECh. 20 - MATHEMATICAL Using the information in Table 20.2,...Ch. 20 - Prob. 9RECh. 20 - Prob. 10RE
Ch. 20 - MATHEMATICAL Calculate E for the following...Ch. 20 - Prob. 12RECh. 20 - MATHEMATICAL Which is more favorable...Ch. 20 - REFLECT AND APPLY Comment on the fact that the...Ch. 20 - RECALL What do cytochromes have in common with...Ch. 20 - RECALL How do the cytochromes differ from...Ch. 20 - RECALL Which of the following does not play a role...Ch. 20 - Prob. 18RECh. 20 - Prob. 19RECh. 20 - REFLECT AND APPLY Two biochemistry students are...Ch. 20 - REFLECT AND APPLY Cytochrome oxidase and...Ch. 20 - Prob. 22RECh. 20 - REFLECT AND APPLY Reflect on the evolutionary...Ch. 20 - REFLECT AND APPLY Experimental evidence strongly...Ch. 20 - Prob. 25RECh. 20 - REFLECT AND APPLY What is the advantage of having...Ch. 20 - REFLECT AND APPLY Why do the electron-transfer...Ch. 20 - Prob. 28RECh. 20 - Prob. 29RECh. 20 - Prob. 30RECh. 20 - RECALL Describe the role of the F1 portion of ATP...Ch. 20 - Prob. 32RECh. 20 - Prob. 33RECh. 20 - Prob. 34RECh. 20 - REFLECT AND APPLY What is the approximate P/O...Ch. 20 - REFLECT AND APPLY Why is it difficult to determine...Ch. 20 - REFLECT AND APPLY What are some of the...Ch. 20 - RECALL Briefly summarize the main arguments of the...Ch. 20 - Prob. 39RECh. 20 - Prob. 40RECh. 20 - Prob. 41RECh. 20 - Prob. 42RECh. 20 - REFLECT AND APPLY Criticize the following...Ch. 20 - Prob. 44RECh. 20 - Prob. 45RECh. 20 - Prob. 46RECh. 20 - RECALL How does the yield of ATP from complete...Ch. 20 - REFLECT AND APPLY The malate-aspartate shuttle...Ch. 20 - MATHEMATICAL What yield of ATP can be expected...Ch. 20 - MATHEMATICAL The free-energy change (G) for the...
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- REFLECT 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_forwardREFLECT AND APPLLY Show how the estimate of 33% efficiency of energy use in anaerobic glycolysis is derived.arrow_forwardMATHEMATICAL 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_forward
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