Peptidoglycan -summary- 02-Oct-10

Peptidoglycan Forms a mesh-like layer outside the plasma

membrane of bacteria forming the cell wall . Peptidoglycan
serves a structural role in the bacterial cell wall, giving
structural strength, as well as counteracting the osmotic
pressure of the cytoplasm.Some antibacterial drugs such as
penicillin interfere with the production of peptidoglycan by
binding to bacterial enzymes known as penicillin-binding
proteins or transpeptidases
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Peptidoglycan, also known as murein, is a polymer consisting of sugars and

amino acids that forms a mesh-like layer outside the plasma membrane of
bacteria (but not Archaea), forming the cell wall. The sugar component
consists of alternating residues of β-(1,4) linked N-acetylglucosamine and N-
acetylmuramic acid. Attached to the N-acetylmuramic acid is a peptide chain
of three to five amino acids. The peptide chain can be cross-linked to the
peptide chain of another strand forming the 3D mesh-like layer. Some
Archaea have a similar layer of pseudopeptidoglycan or pseudomurein, where
the sugar residues are β-(1,3) linked N-acetylglycosamine and N-
acetyltalosaminuronic acid. That is why the cell wall of Archaea is insensitive
to lysozyme.[1] Peptidoglycan serves a structural role in the bacterial
cell wall, giving structural strength, as well as counteracting the
osmotic pressure of the cytoplasm. A common misconception is that
peptidoglycan gives the cell its shape; however, whereas peptidoglycan helps
maintain the structure of the cell, it is actually the MreB protein that
facilitates cell shape. Peptidoglycan is also involved in binary fission during
bacterial cell reproduction

The peptidoglycan layer is substantially thicker in Gram-positive bacteria (20

to 80 nanometers) than in Gram-negative bacteria (7 to 8 nanometers), with
the attachment of the S-layer. Peptidoglycan forms around 90% of the dry
weight of Gram-positive bacteria but only 10% of Gram-negative strains. In
Gram-positive strains, it is important in attachment roles and stereotyping
purposes.[2] For both Gram-positive and Gram-negative bacteria, particles of
approximately 2 nm can pass through the peptidoglycan.[3]
* 1 Structure - * 2 Antibiotic inhibition- * 3 See also * 4 References
* 5 External links
[] Structure
The peptidoglycan layer in the bacterial cell wall is a crystal lattice structure
formed from linear chains of two alternating amino sugars, namely N-
acetylglucosamine (GlcNAc or NAG) and N-acetylmuramic acid (MurNAc or
NAM). The alternating sugars are connected by a β-(1,4)-glycosidic bond.
Each MurNAc is attached to a short (4- to 5-residue) amino acid chain,
containing D-alanine, D-glutamic acid, and meso-diaminopimelic acid in the
case of Escherichia coli (a Gram negative bacteria) or L-alanine, D-glutamine,
L-lysine, and D-alanine in the case of Staphylococcus aureus (a Gram positive
bacteria). These amino acids, except the L-amino acids, do not occur in
proteins and are thought to help protect against attacks by most
peptidases[].
Cross-linking between amino acids in different linear amino sugar chains
occurs with the help of the enzyme transpeptidase and results in a 3-
dimensional structure that is strong and rigid. The specific amino acid
sequence and molecular structure vary with the bacterial species.[4]
[] Antibiotic inhibition
Some antibacterial drugs such as penicillin interfere with the
production of peptidoglycan by binding to bacterial enzymes
known as penicillin-binding proteins or transpeptidases[2].
Penicillin-binding proteins form the bonds between oligopeptide crosslinks in
peptidoglycan. For a bacterial cell to reproduce through binary fission, more
than a million peptidoglycan subunits (NAM-NAG+oligopeptide) must be
attached to existing subunits.[5] Mutations in transpeptidases that lead to
reduced interactions with an antibiotic are a significant source of emerging
antibiotic resistance.[6]
Considered the human body's own antibiotic, lysozymes found in tears work
by breaking the β-(1,4)-glycosidic bonds in peptidoglycan (see below) and
thereby destroying many bacterial cells. Antibiotics such as penicillin
commonly target bacterial cell wall formation (of which peptidoglycan is an
important component) because animal cells do not have cell walls.