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
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Chapter1: Biochemistry: An Evolving Science
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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
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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