Impact of Mutation on Enzyme Functionality

Hard Biochemistry Enzymes

Enzymes are vital biological catalysts that facilitate various biochemical reactions within living organisms. A certain enzyme, hyper-active under acidic conditions, exhibits an optimal pH of 2.5. Research has shown that this enzyme not only catalyzes the breakdown of substrates but also undergoes conformational changes that affect its activity. Recent studies indicate that a point mutation in the enzyme’s active site, which replaces a glutamic acid residue with a valine, affects its binding efficiency and overall catalytic activity. Considering the relationship between enzyme structure and function, which of the following statements best explains the impact of this mutation on the enzyme's functionality?

The replacement of glutamic acid, a charged residue, with valine, a hydrophobic residue, may hinder substrate binding due to reduced ionic interactions.

The mutation enhances the enzyme's stability by creating a more hydrophobic environment around the active site.

The conformational change induced by the mutation allows for a tighter fit of the substrate in the active site.

The mutation does not affect the enzyme activity, as valine can mimic the function of glutamic acid in this context.

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