Introduction
An overview of penicillin-binding proteins (PBPs)
Penicillin-binding proteins (PBPs) are membrane proteins located on the bacterial cell membrane that can bind covalently to penicillin and non-β-lactam antibiotics. PBPs are enzymes involved in the biosynthesis of bacterial cell wall peptidoglycans, including transpeptidase, carboxypeptidase, and endopeptidase. Its normal existence is an essential condition for bacteria to maintain normal morphology and function. PBPs weigh about 1% of the entire cell membrane, and the molecular mass is generally 34.7 to 138.9 ku. Most bacterial cells contain between 10,000 and 10,000 PBPs, one of which usually contains 4 to 8 PBPs, and different bacteria have different types of PBPs.
Major types of PBPs
PBPs are mostly multidomain enzymes divided in three classes (A, B and C) based on their domain organization and function. Besides, according to the sensitivity of bacteria to various β-lactam antibiotics, PBPs can be roughly classified into two categories. The first category is PBPs that are less sensitive to penicillin but sensitive to most cephalosporins, such as PBP4 of S. aureus, PBP5, PBP6 of Escherichia coli. The second category is PBPs that are sensitive to both penicillin and cephalosporins, such as PBP2 and PBP3 of E. coli.
Inhibition of PBPs
Inhibitors of PBPs includes β-Lactam Inhibitors and Non-β-Lactams Inhibitors. Commercially available β-Lactam Inhibitors of PBPs almost exclusively contain the four-membered β-lactam ring, such as Penicillins, Cephalosporins, Carbapenems and Monobactams. Non-β-Lactams inhibitors of PBPs escape the action of β-lactamases but none have yet undergone developments sufficient for initiating clinical trials. The most promising Non-β-Lactams inhibitors of PBPs are lactivicin analogs.
Penicillin-binding proteins (PBPs) are membrane proteins located on the bacterial cell membrane that can bind covalently to penicillin and non-β-lactam antibiotics. PBPs are enzymes involved in the biosynthesis of bacterial cell wall peptidoglycans, including transpeptidase, carboxypeptidase, and endopeptidase. Its normal existence is an essential condition for bacteria to maintain normal morphology and function. PBPs weigh about 1% of the entire cell membrane, and the molecular mass is generally 34.7 to 138.9 ku. Most bacterial cells contain between 10,000 and 10,000 PBPs, one of which usually contains 4 to 8 PBPs, and different bacteria have different types of PBPs.
Major types of PBPs
PBPs are mostly multidomain enzymes divided in three classes (A, B and C) based on their domain organization and function. Besides, according to the sensitivity of bacteria to various β-lactam antibiotics, PBPs can be roughly classified into two categories. The first category is PBPs that are less sensitive to penicillin but sensitive to most cephalosporins, such as PBP4 of S. aureus, PBP5, PBP6 of Escherichia coli. The second category is PBPs that are sensitive to both penicillin and cephalosporins, such as PBP2 and PBP3 of E. coli.
Inhibition of PBPs
Inhibitors of PBPs includes β-Lactam Inhibitors and Non-β-Lactams Inhibitors. Commercially available β-Lactam Inhibitors of PBPs almost exclusively contain the four-membered β-lactam ring, such as Penicillins, Cephalosporins, Carbapenems and Monobactams. Non-β-Lactams inhibitors of PBPs escape the action of β-lactamases but none have yet undergone developments sufficient for initiating clinical trials. The most promising Non-β-Lactams inhibitors of PBPs are lactivicin analogs.
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