Final answer:
The transfer of the nascent peptide chain from the peptidyl-tRNA to aminoacyl-tRNA is catalyzed by peptidyl transferase, a ribosomal enzyme, during protein synthesis.
Step-by-step explanation:
The reaction that allows the nascent chain to be transferred from the peptidyl-tRNA to the aminoacyl-tRNA is known as the peptidyl transferase reaction. This reaction occurs within the ribosome, a cellular machine that synthesizes proteins.
Peptidyl transferase, an enzyme that is actually part of the ribosomal RNA, catalyzes the formation of peptide bonds during the protein elongation process. The energy needed for the peptide bond formation is derived from the high-energy bond that links the amino acid to its tRNA.
Detailed steps include the aminoacyl-tRNA entering the A site and forming a peptide bond with the polypeptide chain attached to the P-site tRNA. This is followed by a series of translocation events where the ribosome moves, the empty tRNA moves to the E site to be expelled, and the tRNA carrying the polypeptide chain moves from the A site to the P site.
Key processes during elongation, such as binding of a charged aminoacyl-tRNA to the A site and translocation, require energy derived from GTP hydrolysis, which is catalyzed by specific elongation factors. Collectively, these intricate events result in the rapid and efficient synthesis of proteins in living organisms.