Suppose that you are working with an enzyme that has an ionizable active site residue with a pk of around 6. The residue must be negatively charged for substrate binding and catalysis to occur. The reaction scheme is shown. +P+ E + A° H 11 EH + S+ = ES → E Which plot shows the expected pH dependency of the reaction velocity (Vo) when [S] = Km ? Drag and drop the correct plot into the axes. Assume that the substrate is positively charged from pH 4 to pH 8 and that the Km was determined at pH 8. max 4 5 6 7 8
Suppose that you are working with an enzyme that has an ionizable active site residue with a pk of around 6. The residue must be negatively charged for substrate binding and catalysis to occur. The reaction scheme is shown. +P+ E + A° H 11 EH + S+ = ES → E Which plot shows the expected pH dependency of the reaction velocity (Vo) when [S] = Km ? Drag and drop the correct plot into the axes. Assume that the substrate is positively charged from pH 4 to pH 8 and that the Km was determined at pH 8. max 4 5 6 7 8
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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![Suppose that you are working with an enzyme that has an ionizable active site residue with a pK₁ of around 6. The residue must
be negatively charged for substrate binding and catalysis to occur. The reaction scheme is shown.
SES
E
+ S+
V
+
H*
11
EH
Which plot shows the expected pH dependency of the reaction velocity (Vo) when [S] = Km ? Drag and drop the correct plot
into the axes. Assume that the substrate is positively charged from pH 4 to pH 8 and that the Km was determined at pH 8.
max
4 5 6 7 8
E +P+
pH
Answer Bank](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fc94cb5d1-997a-49d0-b0ef-9ec02bf0a187%2F4d45a5ca-c048-4b24-9fe2-a3b09702f4ef%2Fodn205d_processed.png&w=3840&q=75)
Transcribed Image Text:Suppose that you are working with an enzyme that has an ionizable active site residue with a pK₁ of around 6. The residue must
be negatively charged for substrate binding and catalysis to occur. The reaction scheme is shown.
SES
E
+ S+
V
+
H*
11
EH
Which plot shows the expected pH dependency of the reaction velocity (Vo) when [S] = Km ? Drag and drop the correct plot
into the axes. Assume that the substrate is positively charged from pH 4 to pH 8 and that the Km was determined at pH 8.
max
4 5 6 7 8
E +P+
pH
Answer Bank
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