Impact of Amino Acid Substitution on Enzyme Activity

Very Hard Organic Chemistry Biological Molecules

In the context of biological molecules, the structural and functional relationship between proteins and their constituent amino acids is paramount. Each amino acid is characterized by a distinctive side chain (R group) that affects its chemical properties and interactions. Consider a hypothetical enzyme that facilitates the conversion of substrate A into product B. This enzyme exhibits an active site specifically designed to accommodate a substrate with a particular side chain structure.

If an experimental mutation occurs, replacing a polar amino acid in the active site with a non-polar amino acid, which of the following outcomes is most likely to result from this modification?

The enzyme's activity increases due to enhanced hydrophobic interactions.

The enzyme becomes completely inactive due to loss of specific substrate binding.

The enzyme's reaction rate remains unchanged as non-polar amino acids can participate equally in reactions.

The enzyme's substrate specificity shifts to accommodate non-polar substrates.

Hint

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