Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Question
Chapter 9, Problem 16P
Interpretation Introduction
Interpretation:
The activity of the version of subtilisin with all three residues in the catalytic triad have compared to uncatalyzed reaction is to be stated with an explanation.
Concept introduction:
The biological catalysts which lower the minimum amount of energy required by the reactants to convert into product are known as enzymes. An enzyme does not alter the potential energy of reactant and product. Proteolytic enzymes commonly known as proteases are used for the cleavage of protein.
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Chemical labeling of chymotrypsin by the compound tosylphenylalanine chloromethyl ketone (TPCK) modifies the His 57 in the
enzyme's active site. The structure of this derivative is shown below. TPCK inactivates the enzyme because the bulky addition
prevents it from cleaving nearby covalent bonds.
HCI
+ CH,
C-O
Chymotrypsin-His 57 TPCK
Modified enzyme
True
O False
ENZYME KINETICS ANALYSIS
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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
not true about the Michaelis-Menten equation?
The equation that gives the rate, v, of an
the substrate concentration [S] is the Michaelis-Menten equation
= Vmax[S]/(Km + [S]), where V,
enzyme-catalyzed reaction for all values of
max and Km are constants. Which of the following is
a)
for [S] << Km, V = Vmax
applies to most enzymes, but allosteric enzymes have different kinetics
when [S] = Km, then v =
Vmax/2
gives the rate when the enzyme concentration, temperature, pH, and ionic
strength are constant
for very high values of [S], v approaches Vmax
e)
Which is correct about the constant Km in the Michaelis-Menten equation?
also called the catalytic constant or turnover number
equal to the number of product molecules produced per unit time when the
enzyme is saturated with substrate
it is the constant in the first order rate equation v = k[A]
it is the constant in the second order rate equation v =
equal to the substrate concentration at which the velocity or rate of a reaction is
½ the…
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