The bacterial cell wall is formed ofa)Celluloseb)Hemicellulosec)Peptid...
Peptidoglycan, also known as murein, is a polymer consisting of sugars and amino acids that forms a mesh-like layer outside theplasma membraneof most bacteria, forming the cell wall. The sugar component consists of alternating residues of β-(1,4) linked Nacetylglucosamine(NAG) and N-acetylmuramic acid (NAM) . Attached to the N-acetylmuramic acid is a peptide chain of three tofive amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer.[1]Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmoticpressure of the cytoplasm. A common misconception is that peptidoglycan gives the cell its shape; however, whereas peptidoglycanhelps maintain the structural strength of the cell, it is actually the MreB protein that facilitates cell shape.[2][3][4] Peptidoglycan is alsoinvolved in binary fission during bacterial cell reproduction.The peptidoglycan layer is substantially thicker in Gram-positivebacteria (20 to 80 nanometers) than in Gram-negative bacteria (7 to8 nanometers), with the attachment of the S-layer. Peptidoglycan forms around 90%The structure of peptidoglycan. NAG = N-acetylglucosamine(also called GlcNAc or NAGA), NAM = N-acetylmuramic acid(also called MurNAc or NAMA).Gram-positivecell wallPenicillin binding protein forming cross-links in newly formedbacterial cell wall.The peptidoglycan monomers are synthesized in the cytosol and are then attached to a membrane carrier bactoprenol. Bactoprenoltransports peptidoglycan monomers across the cell membrane where they are inserted into the existing peptidoglycan. [9]In the first step of peptidoglycan synthesis, glutamine, which is an amino acid, donates an amino group to a sugar, fructose 6-phosphate. This turns fructose 6-phosphate into glucosamine-6-phosphate. In step two, an acetyl group is transferred from acetyl CoAto the amino group on the glucosamine-6-phosphate creating N-acetyl-glucosamine-6-phosphate.[10] In step three of the synthesisprocess, the N-acetyl-glucosamine-6-phosphate is isomerized, which will change N-acetyl-glucosamine-6-phosphate to N-acetylglucosamine-1-phosphate.[10]In step 4, the N-acetyl-glucosamine-1-phosphate, which is now a monophosphate, attacks UTP. Uridine triphosphate, which is apyrimidine nucleotide, has the ability to act as an energy source. In this particular reaction, after the monophosphate has attacked theUTP, an inorganic pyrophosphate is given off and is replaced by the monophosphate, creating UDP-N-acetylglucosamine (2,4).(When UDP is used as an energy source, it gives off an inorganic phosphate.) This initial stage, is used to create the precursor for theNAG in peptidoglycan.In step 5, some of the UDP-N-acetylglucosamine (UDP-GlcNAc) is converted to UDP-MurNAc (UDP-N-acetylmuramic acid) by theaddition of a lactyl group to the glucosamine. Also in this reaction, the C3 hydroxyl group will remove a phosphate from the alphacarbon of phosphoenolpyruvate. This creates what is called an enol derivative that will be reduced to a “lactyl moiety” by NADPH instep six.[10]In step 7, the UDP–MurNAc is converted to UDP-MurNAc pentapeptide by the addition of five amino acids, usually including thedipeptide D-alanyl-D-alanine.[10] Each of these reactions requires the energy source ATP.[10] This is all referred to as Stage one.Stage two occurs in the cytoplasmic membrane. It is in the membrane where a lipid carrier called bactoprenol carries peptidoglycanprecursors through the cell membrane. Bactoprenol will attack the UDP-MurNAc penta, creating a PP-MurNac penta, which is now alipid. UDP-GlcNAc is then transported to MurNAc, creating Lipid-PP-MurNAc penta-GlcNAc, a disaccharide, also a precursor topeptidoglycan.[10] How this molecule is transported through the membrane is still not understood. However, once it is there, it isadded to the growing glycan chain.[10] The next reaction is known as tranglycosylation. In the reaction, the hydroxyl group of theGlcNAc will attach to the MurNAc in the glycan, which will displace the lipid-PP from the glycan chain. The enzyme responsible forthis is transglycosylase.[10]Some antibacterial drugssuch as penicillin interfere with the production of peptidoglycan by binding to bacterial enzymes known aspenicillin-binding proteins or DD-transpeptidases.[6] Penicillin-binding proteins form the bonds between oligopeptide crosslinks inpeptidoglycan. For a bacterial cell to reproduce through binary fission, more than a million peptidoglycan subunits (NAMNAG+oligopeptide)must be attached to existing subunits.[11] Mutations in genes coding for transpeptidases that lead to reducedinteractions with an antibiotic are a significant source of emerging antibiotic resistance.[12]Lysozyme, which is found in tears and constitutes part of the body's innate immune system exerts its antibacterial effect by breakingthe β-(1,4)-glycosidic bonds in peptidoglycan (see above).Some archaea have a similar layer of pseudopeptidoglycan (also known as pseudomurein), in which the sugar residues are β-(1,3)linked N-acetylglucosamine and N-acetyltalosaminuronic acid. This makes the cell walls of such archaea insensitive to lysozyme