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Peptidoglycan is the major component of the cell envelope of virtually all bacteria.Moreover, C55-P is also shared by other cell wall pathways, such as the wall teichoic acid synthesis and capsular polysaccharide synthesis in Staphylococcus aureus [11,12,13,14].MraY catalyzes the first membrane step of peptidoglycan synthesis by transferring the phospho-MurNAc-pentapeptide moiety from UDP-Mpp to C55-P and yields uridine-monophosphate (UMP) and undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, typically referred to as Lipid I [8].Although the use of C55-P as the lipid carrier is the common rule in bacteria, there is evidence that the shorter chain decaprenyl phosphate and nonaprenyl phosphate homologues assist glycan translocation in some species [9,10].After Lipid I synthesis, the glycosyltransferase MurG transfers a GlcNAc moiety from UDP-GlcNAc to Lipid I to produce undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)- GlcNAc.A number of proteins involved in this pathway, such as the Mur enzymes and the penicillin binding proteins (PBPs), have been studied and regarded as good targets for antibiotics.
Peptidoglycan is the major component of the cell envelope of virtually all bacteria.
It has structural roles and acts as a selective sieve for molecules from the outer environment.
Peptidoglycan synthesis is therefore one of the most important biogenesis pathways in bacteria and has been studied extensively over the last twenty years.
A number of proteins involved in this pathway, such as the Mur enzymes and the penicillin binding proteins (PBPs), have been studied and regarded as good targets for antibiotics.
The present review focuses on the membrane steps of peptidoglycan synthesis that involve two enzymes, MraY and MurG, the inhibitors of these enzymes and the inhibition mechanisms.
We also discuss the challenges of targeting these two cytoplasmic membrane (associated) proteins in bacterial cells and the perspectives on how to overcome the issues.
UDP-Mpp and C55-P are the two substrates of the integral membrane enzyme phospho-MurNAc-pentapeptide translocase (MraY).
MraY catalyzes the first membrane step of peptidoglycan synthesis by transferring the phospho-MurNAc-pentapeptide moiety from UDP-Mpp to C55-P and yields uridine-monophosphate (UMP) and undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, typically referred to as Lipid I [8].
Although the use of C55-P as the lipid carrier is the common rule in bacteria, there is evidence that the shorter chain decaprenyl phosphate and nonaprenyl phosphate homologues assist glycan translocation in some species [9,10].
Moreover, C55-P is also shared by other cell wall pathways, such as the wall teichoic acid synthesis and capsular polysaccharide synthesis in Staphylococcus aureus [11,12,13,14].
Since C55-P exists in bacterial cells in very limited amounts, the synthesis of these different components is highly integrated and coordinated temporally.
After Lipid I synthesis, the glycosyltransferase MurG transfers a GlcNAc moiety from UDP-GlcNAc to Lipid I to produce undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)- GlcNAc.
This is usually referred to as Lipid II, which is subsequently transported by a flippase from the inner side of the membrane to the outer side [15,16,17,18] where polymerization to give a peptidoglycan layer takes place.
The proteins that catalyze the last steps of the formation of the peptidoglycan layer have been researched in
تلخيص النصوص العربية والإنجليزية اليا باستخدام الخوارزميات الإحصائية وترتيب وأهمية الجمل في النص
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