Chloramphenicol's mechanism of action involves inhibition of which enzymatic activity?

Chloramphenicol exerts its antimicrobial effects primarily through the inhibition of peptidyl transferase activity in bacterial ribosomes. This mechanism involves binding to the 50S subunit of the bacterial ribosome, specifically blocking the peptidyl transferase center. As a result, the formation of peptide bonds between amino acids during protein synthesis is disrupted. This inhibition effectively halts bacterial growth and replication, rendering chloramphenicol a potent antibiotic.

Understanding this mechanism is crucial in pharmacology and microbiology, as it highlights how chloramphenicol selectively targets bacterial protein synthesis, distinguishing it from the action of other antibiotics that may act on different parts of the bacterial ribosome or target other cellular processes. This specificity underlines its clinical utility, especially in treating serious infections when other antibiotics may not be effective.