This table provides enzyme reactions (initial rate, V0) from experiments of food technologist on glucoamylase, used at various concentrations of substrates in solutions with [E] = 1.2 x 10-4 mmol/L. Enzyme kinetics of glucoamylase is a function of substrate concentration with the presence or absence of 2 mM inhibitors. With Inhibitors [S] (mmol/L) Without Inhibitors Vo (mmol/L-min) V₁ (mmol/L-min) 0.710 0.200 0.180 0.400 0.180 0.150 0.310 0.160 0.110 0.098 0.120 0.070 0.066 0.400 0.050 0.040 0.070 0.040 a) Draw the graph of the relationship between the substrate concentration on the reaction rate, the Lineweaver-Burk equation, with no and no inhibitors! b) Use the data from without inhibitors to calculate Vmax, and Km for this enzyme- catalysed reaction c) Use the data from with Inhibitor to determine the apparent Vmax and Km in the presence of the inhibitor. Determine the type of inhibition (competitive, non- competitive or uncompetitive)
This table provides enzyme reactions (initial rate, V0) from experiments of food technologist on glucoamylase, used at various concentrations of substrates in solutions with [E] = 1.2 x 10-4 mmol/L. Enzyme kinetics of glucoamylase is a function of substrate concentration with the presence or absence of 2 mM inhibitors. With Inhibitors [S] (mmol/L) Without Inhibitors Vo (mmol/L-min) V₁ (mmol/L-min) 0.710 0.200 0.180 0.400 0.180 0.150 0.310 0.160 0.110 0.098 0.120 0.070 0.066 0.400 0.050 0.040 0.070 0.040 a) Draw the graph of the relationship between the substrate concentration on the reaction rate, the Lineweaver-Burk equation, with no and no inhibitors! b) Use the data from without inhibitors to calculate Vmax, and Km for this enzyme- catalysed reaction c) Use the data from with Inhibitor to determine the apparent Vmax and Km in the presence of the inhibitor. Determine the type of inhibition (competitive, non- competitive or uncompetitive)
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Assignment Session 8 & 9
This table provides enzyme reactions (initial rate, V0) from experiments of food
technologist on glucoamylase, used at various concentrations of substrates in solutions
with [E] = 1.2 x 10-4 mmol/L. Enzyme kinetics of glucoamylase is a function of
substrate concentration with the presence or absence of 2 mM inhibitors.
Without Inhibitors.
With Inhibitors
[S] (mmol/L)
Vo (mmol/L-min)
V₁ (mmol/L-min)
0.710
0.200
0.180
0.400
0.180
0.150
0.310
0.160
0.110
0.098
0.120
0.070
0.066
0.400
0.050
0.040
0.070
0.040
a) Draw the graph of the relationship between the substrate concentration on the
reaction rate, the Lineweaver-Burk equation, with no and no inhibitors!
b) Use the data from without inhibitors to calculate Vmax, and Km for this enzyme-
catalysed reaction
c) Use the data from with Inhibitor to determine the apparent Vmax and Km in the
presence of the inhibitor. Determine the type of inhibition (competitive, non-
competitive or uncompetitive)
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Transcribed Image Text:3
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Assignment Session 8 & 9
This table provides enzyme reactions (initial rate, V0) from experiments of food
technologist on glucoamylase, used at various concentrations of substrates in solutions
with [E] = 1.2 x 10-4 mmol/L. Enzyme kinetics of glucoamylase is a function of
substrate concentration with the presence or absence of 2 mM inhibitors.
Without Inhibitors.
With Inhibitors
[S] (mmol/L)
Vo (mmol/L-min)
V₁ (mmol/L-min)
0.710
0.200
0.180
0.400
0.180
0.150
0.310
0.160
0.110
0.098
0.120
0.070
0.066
0.400
0.050
0.040
0.070
0.040
a) Draw the graph of the relationship between the substrate concentration on the
reaction rate, the Lineweaver-Burk equation, with no and no inhibitors!
b) Use the data from without inhibitors to calculate Vmax, and Km for this enzyme-
catalysed reaction
c) Use the data from with Inhibitor to determine the apparent Vmax and Km in the
presence of the inhibitor. Determine the type of inhibition (competitive, non-
competitive or uncompetitive)
MacBook Pro
(
$
&
7
4
R
%
5
0,
T
A
6
Y
U
14
* 00
8
-
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