Peptidoglycan synthesis enzyme (Staphylococcus aureus)

Peptidoglycan synthesis enzymes in Staphylococcus aureus catalyze the polymerization of peptidoglycan, crucial for the bacterial cell wall, morphogenesis, and survival. They are well-established targets for multiple antibiotic classes including β-lactams and glycopeptides, which inhibit key steps in cell wall formation, leading to cell death. Chelerythrine, a benzophenanthridine alkaloid, has been shown to exert antibacterial activity against S. aureus via disruption of the cell wall and membrane, but its direct molecular binding partner within the cell wall synthesis pathway remains less well-defined compared to canonical antibiotics such as β-lactams. Selectivity and toxicity remain concerns for chelerythrine’s therapeutic use. Important clarification: The phrase provided is not a molecular target/receptor name but a description of a process affected by chelerythrine. If a specific enzyme or protein within the S. aureus cell wall synthesis pathway is identified as chelerythrine’s direct target in future literature, that should replace the current entry. For now, the above structured form is the closest accurate standardization based on available information.

Other names

Peptidoglycan synthaseCell wall biosynthesis enzymePenicillin-binding protein (general, if exact PBP is not specified)

Inhibition of peptidoglycan synthesis; Disruption of bacterial cell wall integrity, leading to bacterial lysis and death; In the case of chelerythrine specifically, direct disruption of bacterial cell wall and membrane