Penicillin binding protein
Penicillin binding protein (PBP’s) refers to protein group that are characterized by the similarity for and binding of penicillin. Additionally, it is also a typical bacterium constituent and the name is a reflection of the manner through which this protein was discovered. The function of PBP’s involves mediation removal of D-alanine from precursors. There are different kinds of PBPs and their names often have a number that is related to their molecular weight.
This protein has also attracted great attention from scientists attributed to the fact synthesis of bacterial wall is the major target of most antibiotics. Note that the PBP’s number is often large with several in every organism. Additionally, these can be found as cytoplasmic proteins and membrane bound. For instance in the reports made by Spratt in 1977, there are 6 varying PBP’s which are detected routinely in all E. coli strains and they range in molecular weight from forty thousand to ninety one thousand.
These varying PBPs occur in varying numbers in each cell and they also have different penicillin affinities. Ideally, these can be classified into two classes which include low molecular weight (LMW) and high-molecular weight (HMW) categories. Proteins which have already evolved from PBP will be noted in high organisms and this might include in the LACTB protein of the mammalian.
PBPs are used during the final synthesis stages of peptidoglycan which is a very important element of bacterial walls. For growth to take place, cell division or maintenance of cellular bacterial structure, then wall synthesis of bacterial cell of great importance. If there is inhibition of any kind regardless of how slight, then irregularities in the structure of the cell wall arises and this might include lesions, elongation, eventual death of cells, lysis as well as cell call irregularities in structure. It is important to note PBP’s catalyze a couple of reactions which are part of the synthesizing cross link peptidoglycan.
PBP’s are known to bind β-lactam for the simple reason the two have a chemical structure that is similar to modular pieces forming the peptidoglycan. Consequently, once they bind with penicillin there is rupture of the β-lactam amide bond forming a covalent bond which has a serine catalytic residue at the active site of the PBPs. Note the reaction cannot be reversed and it also leads to inactivation of the enzyme.
A lot of research has been carried out on PBPs largely because of the role they play in resistance as well as antibiotics. Bacterial synthesis of the cell wall and the function played by PBPs is of great importance for drugs as well as selective toxicity because of metabolic enzymes and pathways that are distinctive to bacteria.
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