Final answer:
The presence of hydroxyl groups (-OH) on the side chains of serine, threonine, and tyrosine allows these amino acids to be phosphorylated. Enzymes known as kinases catalyze the addition of a phosphate group from ATP, altering the protein's function. Phosphatases can reverse this process by removing the phosphate group.
The correct answer is option d) Presence of hydroxyl groups
Step-by-step explanation:
The property that enables the residues of the amino acids serine, threonine, and tyrosine to be phosphorylated is the presence of hydroxyl groups. These specific amino acids contain a hydroxyl group (-OH) in their side chains, which can undergo a reaction with a phosphate group to form a phosphorylated amino acid. This process is typically catalyzed by enzymes called kinases, which transfer a phosphate group from ATP to the hydroxyl group of the amino acid, a key step in protein phosphorylation, an important type of post-translational modification (PTM).
Phosphorylation usually results in a change in the activity or function of the protein, often activating or deactivating it or altering its ability to interact with other molecules. The reversal of phosphorylation, which involves the removal of a phosphate group, is carried out by another class of enzymes called phosphatases.