100 75 50 25 7 6. 11 pH % enzyme activity 3.
Anatomy & Physiology
1st Edition
ISBN:9781938168130
Author:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble
Publisher:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble
Chapter2: The Chemical Level Of Organization
Section: Chapter Questions
Problem 39CTQ: AB+CDAD+BE Is this a legitimate example of an exchange reaction? Why or why not?
Related questions
Question
An enzyme contains an active site aspartic acid with a pKa = 5.0, which
acts as a general acid catalyst. On the accompanying template, draw the
curve of enzyme activity (reaction rate) versus pH for the enzyme (assume
that the protein is stably folded between pH 2–12 and that the active site
Asp is the only ionizable residue involved in catalysis). Briefly explain the
shape of your curve.
Transcribed Image Text:100
75
50
25
7
6.
11
pH
% enzyme activity
3.
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