Sandbox 126: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 11: | Line 11: | ||
==='''Mechanism of action of Beta-Lactam Antibiotics'''=== | ==='''Mechanism of action of Beta-Lactam Antibiotics'''=== | ||
The beta-lactam antibiotics irreversibly bind to and inhibit TPs. This results in the disruption of peptidoglycan synthesis and ultimately cell growth. Specifically, beta-lactams, such as penicillin and the anti-MRSA cephlasporins, ceftobiprole and ceftaroline, are molecular mimics of the peptidoglycan D-Ala-D-Ala moiety; the normal TP substrate (Figure 2; Tipper and Strominger, 1965). Therefore, they "trick" the TP active site serine residue to react with them, resulting in the irreversible inhibition of TP activity and of cell wall synthesis. | The beta-lactam antibiotics irreversibly bind to and inhibit TPs. This results in the disruption of peptidoglycan synthesis and ultimately cell growth. Specifically, beta-lactams, such as penicillin and the anti-MRSA cephlasporins, ceftobiprole and ceftaroline, are molecular mimics of the peptidoglycan D-Ala-D-Ala moiety; the normal TP substrate (Figure 2; Tipper and Strominger, 1965). Therefore, they "trick" the TP active site serine residue to react with them, resulting in the irreversible inhibition of TP activity and of cell wall synthesis.[[Image: MechanismofPBP.jpg|thumb|alt= Alt text|Figure 2. Schematic showing Catalytic Mechanism of PBP2a |550px]] | ||
==='''MRSA, PBP2a, and anti-MRSA Cephalosporins'''=== | ==='''MRSA, PBP2a, and anti-MRSA Cephalosporins'''=== | ||
