4. Determine the V. Ka and k for the enzyme. Is this enzyme approaching catalytical perfection? Identify the typefs) of inhibition for 2 & 3. Can the inhibition be overcome by addition of substrate? Explain your conclusions.

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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4

The following table indicates the rates at which a substrate reacts as catalyzed by an enzyme that follows
the Michaelis-Menten mechanism: (1) in the absence of inhibitor, (2) and (3) in the presence of 10mM
concentration respectively, of cach of two inhibitors. [Er]=2nM and assume Er is the same for all
INFORMATION
reactions
140
o 1/ve y=0.9989x + 0.3001
D ve
10
o1 ve a
1.20
1.00
y=0.7541x + 0.1
80
0.60
y=0.3017x+0.0987
0.40
2.
DA
0.20
0.00
10
15
20
25
0.20 0.40 0,60
1/[S)
0.00
0.80 1.00
1.20
[S) mM
4. Determine the V, Ka and k for the enzyme. Is this enzyme approaching catalytical perfection?
5. Identify the type(s) of inhibition for 2 & 3. Can the inhibition be overcome by addition of substrate?
Explain your conclusions.
s/wn on
Transcribed Image Text:The following table indicates the rates at which a substrate reacts as catalyzed by an enzyme that follows the Michaelis-Menten mechanism: (1) in the absence of inhibitor, (2) and (3) in the presence of 10mM concentration respectively, of cach of two inhibitors. [Er]=2nM and assume Er is the same for all INFORMATION reactions 140 o 1/ve y=0.9989x + 0.3001 D ve 10 o1 ve a 1.20 1.00 y=0.7541x + 0.1 80 0.60 y=0.3017x+0.0987 0.40 2. DA 0.20 0.00 10 15 20 25 0.20 0.40 0,60 1/[S) 0.00 0.80 1.00 1.20 [S) mM 4. Determine the V, Ka and k for the enzyme. Is this enzyme approaching catalytical perfection? 5. Identify the type(s) of inhibition for 2 & 3. Can the inhibition be overcome by addition of substrate? Explain your conclusions. s/wn on
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