If an amino acid involved in the ability of an enzyme to bind a substrate were changed from a tyrosine to a phenylalanine, what would happen to the enzyme?

Question

Quizplus · Accepted Answer

The change of tyrosine to phenylalanine involves the substitution of a hydroxyl (-OH) group in the side chain of tyrosine with a hydrogen (-H) group in the side chain of phenylalanine. This change in the R-group may affect the interaction between the enzyme and its substrate, as the hydroxyl group is involved in hydrogen bonding and other interactions that contribute to substrate binding. Therefore, the ability of the substrate to bind to the enzyme would be affected because of the change in R groups. The other answer choices are incorrect: A is false because the two amino acids have different properties; B is false because the change does not involve the formation of disulfide bonds; C is false because the two amino acids have non-polar side chains; and D is false because the change is in a single amino acid and not in the entire quaternary structure of the enzyme.

If an Amino Acid Involved in the Ability of an Enzyme