Sandbox 126: Difference between revisions

Line 11:

==='''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.[[Image: MechanismofPBP.jpg|thumb|alt= Alt text|Figure 2. Schematic showing Catalytic Mechanism of PBP2a |550px]]

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 (A) the peptidoglycan |550px]]

==='''MRSA, PBP2a, and anti-MRSA Cephalosporins'''===

Sandbox 126: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 11: / Line 11: @@
 ==='''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.[[Image: MechanismofPBP.jpg|thumb|alt= Alt text|Figure 2. Schematic showing Catalytic Mechanism of PBP2a |550px]]
+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 (A) the peptidoglycan |550px]]
 ==='''MRSA, PBP2a, and anti-MRSA Cephalosporins'''===