All β-lactam antibiotics (except for tabtoxinine-β-lactam, which inhibits glutamine synthetase) bind to PBPs, which are essential for bacterial cell wall synthesis.
Low Molecular-Mass (LMM) PBP’s are dispensable for normal cell growth and control how tightly the peptidoglycan chains are linked together.
[6] PBPs are all involved in the final stages of the synthesis of peptidoglycan, which is the major component of bacterial cell walls.
[3] The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (involved in formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (involved in cross-linking of the peptide subunits) and the serine at the active site is conserved in all members of the PBP family.
[8] In contrast, high-molecular-weight PBPs are independent from MreB and maintain cell wall integrity by detecting and repairing defects in the peptidoglycan.
[9] PBPs bind to β-lactam antibiotics because they are similar in chemical structure to the modular pieces that form the peptidoglycan.
[13] Penicillin binding protein 3 is important for bacteria wall synthesis and is a main target in β-lactam antibiotics.
[5] The active site is located in a long cleft running parallel with the 3 strand across the lower part of the transpeptidase domain.