Peptidoglycan

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Peptidoglycan, also known as murein, is a polymer consisting of sugars and amino acids that forms a homogeneous layer outside the plasma membrane of eubacteria. Some Archaea have a similar layer of pseudopeptidoglycan. Peptidoglycan serves a structural role in the bacterial cell wall, giving the wall shape and structural strength, as well as counteracting the osmotic pressure of the cytoplasm. Peptidoglycan is also involved in binary fission during bacterial cell reproduction.<ref>Madigan M; Martinko J (editors). (2005). Brock Biology of Microorganisms, 11th ed., Prentice Hall. ISBN 0-13-144329-1.</ref>

The peptidoglycan layer is substantially thicker in Gram-positive bacteria (20 to 80 nm) than in Gram-negative bacteria (7 to 8 nm), 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.<ref name=Salton1996>Salton MRJ, Kim KS (1996). Structure. In: Baron's Medical Microbiology (Barron S et al, eds.), 4th ed., Univ of Texas Medical Branch. (via NCBI Bookshelf) ISBN 0-9631172-1-1.</ref>

1 Antibiotic inhibition
2 Structure
3 References
4 External links

[edit] Antibiotic inhibition

Antibacterial drugs such as penicillin target the peptidoglycan layer by interfering with its formation, specifically the crosslinking enzymes transpeptidases<ref name=Salton1996 />. Transpeptidases form the bonds between oligopeptide chains seen in the diagram below. Mutations in the transpeptidase enzymes (also known as penicillin binding proteins or PBPs) which lead to reduced interactions between an antibiotic and the bacterial PBPs are a significant cause of emerging antibiotic resistance.<ref>Spratt BG (1994). "Resistance to antibiotics mediated by target alterations". Science 264 (5157): 388-93. PMID 8153626.</ref>

[edit] Structure

Image:Muréine.JPG

The peptidoglycan layer in the bacterial cell wall is a crystal lattice structure formed from linear chains of two alternating amino sugars, namely N-acetyl glucosamine (GlcNAc or NAG) and N-acetyl muramic acid (MurNAc or NAM). Each MurNAc is attached to a short (4 to 5 residue) amino acid chain, normally containing D-alanine, D-glutamic acid and mesodiaminopimelic acid. These three 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 by an enzyme known as transpeptidase result in a 3-dimensional structure that is strong and rigid. The specific amino acid sequence and molecular structure vary with the bacterial species.<ref>Ryan KJ; Ray CG (editors) (2004). Sherris Medical Microbiology, 4th ed., McGraw Hill. ISBN 0-8385-8529-9.</ref>