Peptidyl transferase

Definition

Peptidyl transferase is an enzyme that forms peptide bonds between adjacent amino acids during protein synthesis. It is a critical component of the ribosome's large subunit.

5 Must Know Facts For Your Next Test

1. Peptidyl transferase activity is essential for elongation during translation.
2. The enzyme catalyzes the formation of peptide bonds in the ribosome, linking amino acids together.
3. It is part of the ribosomal RNA (rRNA) in the large subunit, not a separate protein.
4. Antibiotics like chloramphenicol and macrolides target peptidyl transferase to inhibit bacterial growth.
5. Mutations affecting peptidyl transferase can lead to defects in protein synthesis and are often lethal.

Review Questions

• What role does peptidyl transferase play in protein synthesis?
• How does peptidyl transferase contribute to the formation of peptide bonds?
• Why are certain antibiotics targeting peptidyl transferase effective against bacteria?

Related terms

Ribosome:

A molecular machine responsible for synthesizing proteins by translating mRNA into polypeptides.

rRNA (ribosomal RNA): RNA molecules that form the core structural and functional components of ribosomes.

Translation Elongation: The stage of protein synthesis where amino acids are sequentially added to a growing polypeptide chain.