Penicillin-binding Proteins in Bacteria

Penicillin-binding proteins (PBPs) are bacterial proteins that play a crucial role in the cell wall synthesis of bacteria. They are the target of beta-lactam antibiotics like penicillins and cephalosporins.
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Prepared by Shruti Sahoo, reviewed by Dr. Eugene Smith

Penicillin-binding Proteins FAQ

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What are penicillin-binding proteins?

Erin E. Carlson, in Methods in Enzymology, 2020 Penicillin-binding proteins (PBPs) are membrane-associated proteins involved in the biosynthesis of peptidoglycan (PG), the main component of bacterial cell walls. These proteins were discovered and named for their affinity to bind the β-lactam antibiotic penicillin.

What are penicillin-binding proteins (PBPs)?

(NAM = N-acetylmuramic acid; NAG = N-acetylglucosamine) Penicillin-binding proteins ( PBP s) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered.

Why do penicillin-binding proteins bind -lactam antibiotics?

Penicillin-binding proteins are generally enzymes involved in peptidoglycan biosynthesis, so contribute essential roles in bacterial cell wall biosynthesis. PBPs bind β-lactam antibiotics because their chemical structure is similar to that of the sugar–amino acid backbone that forms peptidoglycan.

How does penicillin interact with a bacterial cell?

Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes. Distinct penicillin-binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Penicillin-binding proteins and cell shape in Escherichia coli.

Penicillin-binding Proteins References

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