Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Question
Chapter 18, Problem 12P
Interpretation Introduction
To analyze:
The free energy observed in the reaction.
Introduction:
The energy which allows predicting the reaction spontaneously at a particular temperature is called free energy. In enolase reaction, free energy changes accordingly.
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6-25
substrate-band enzyme concentrations. The the
turnover number is equal to umax-
b)
V=Umax •57(Km+S)
anstont
For an enzyme that displays Michaelis-Menten kinetics, what is
the reaction velocity, V (as a percentage of Vmax), observed at
the following values?
a)
[S] = KM
C)
d)
e)
[S] = 0.5KM
[S] = = 0.1KM
[S] = 2KM
[S] = 10KM
w
reactores
-maximumrate of reaction
boteles conc.
Would you expect the structure of a competitive inhibitor of a
given enzyme to be similar to that of its substrate?
O BIOCHEMISTRY
Understanding major biochemical energy storage and release.
A certain anabolic biochemical reaction A has AG- 17.8 kJ mol , and is always coupled to another reaction B, which has two reactants and two products, I
this:
R + R2
P + P2
The molecule in the drawing area below is either R, or P.
• If it's R, change it into P. But if it's P, change it into R.
• In either case, draw the molecule as it would exist at physiological pH.
• Also please answer the questions about Reaction B in the table below.
OR,
Was the molecule in the drawing area R, or P, before you changed it?
What is R?
Enter its common name, usual symbol, or chemical formula:
What is P2?
Enter its common name, usual symbol, or chemical formula:
O BIOCHEMISTRY
Understanding major biochemical energy storage and release..
ODO
its common name, usual symbol, or chemical formula:
NH,
-CH
N.
H
OH
OH
......
to
III
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 18 Solutions
Biochemistry
Ch. 18 - Characterizing Glycolysis List the reactions of...Ch. 18 - Radiotracer Labeling of Pyruvate from Glucose...Ch. 18 - Effects of Changing Metabolite Concentrations on...Ch. 18 - Prob. 4PCh. 18 - Prob. 5PCh. 18 - The Reactions and Meehanisms of the Leloir Pathway...Ch. 18 - The Effect of lodoacetic Acid on the...Ch. 18 - Prob. 8PCh. 18 - Comparing Glycolysis Entry Points for Sucrose...Ch. 18 - Prob. 10P
Ch. 18 - Prob. 11PCh. 18 - Prob. 12PCh. 18 - Prob. 13PCh. 18 - Energetic of Fructose-1 ,6-bis P Hydrolysis...Ch. 18 - Prob. 15PCh. 18 - Energetics of the Hexokinase Reaction The...Ch. 18 - Prob. 17PCh. 18 - Distinguishing the Mechanisms of Class I and Class...Ch. 18 - Prob. 19PCh. 18 - Understanding the Mechanism of Hemolytic Anemia...Ch. 18 - Prob. 21PCh. 18 - Based on your residing of this chapter, what would...Ch. 18 - Examine the ActiveModel for alcohol dehydrogenase...Ch. 18 - Based on your knowledge of the structure of NAD+...Ch. 18 - Using the ActiveModel for phosphofructokinase...
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