When the active site of an enzyme is phosphorylated on one of its catalytic amino acid residues, the overall _______________ charge of phosphate groups would _____________ the affinity for a polar, negatively charged substrate.
A
positive; lower.
B
negative; lower.
C
negative; increase.
D
positive; increase.
E
positive; not change.
F
neutral; not change.
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1
Identify the nature of the phosphate group: Phosphate groups carry a negative charge due to their chemical structure.
Consider the effect of adding a negatively charged phosphate group to the enzyme's active site: This will increase the overall negative charge of the active site.
Analyze how the increased negative charge at the active site affects the interaction with a polar, negatively charged substrate: Like charges repel each other, so the increased negative charge will likely decrease the affinity for a negatively charged substrate.
Review the options provided: We are looking for an option that describes an increase in negative charge and a decrease in affinity.
Select the correct answer based on the analysis: The correct choice is 'negative; lower', indicating that the phosphorylation increases the negative charge and lowers the affinity for the negatively charged substrate.