Final answer:
Peptidyl transferase catalyzes the peptide bond formation between amino acids during protein synthesis, occurring within the ribosome's 50S subunit. The enzyme's function is critical for building the polypeptide chain that will eventually fold into a functional protein.
Step-by-step explanation:
The role of peptidyl transferase is to catalyze the peptide bond formation between amino acids during the process of protein synthesis. This enzyme is a component of the ribosome, specifically integrated into the 50S ribosomal subunit. During translation elongation, peptidyl transferase facilitates the formation of a peptide bond between the amino group of the amino acid attached to the A-site tRNA and the carboxyl group of the amino acid attached to the P-site tRNA that is linked to the growing polypeptide chain.
The reaction that peptidyl transferase catalyzes is fundamental for the synthesis of proteins, as it allows for the sequential addition of amino acids to the nascent polypeptide chain. This enzyme does not require energy from GTP hydrolysis for peptide bond formation; instead, the energy is derived from the high-energy bond linking the amino acid to its tRNA.