Peptidoglycan: Difference between revisions

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[[Penicillin|Penicillin]] [[Inhibits|inhibits]] the effect of peptidoglycan in&nbsp;bacteria by binding to [[Serine|serine]] in the enzyme [[Glycopeptide transpeptidase|glycopeptide transpeptidase]].&nbsp;As a result,&nbsp;it&nbsp;can no longer catalyse the formation of cross-links.&nbsp;The enzyme is irreversibly inhibitted which therefore results&nbsp;in the termination of bacterial growth<ref>http://www.ncbi.nlm.nih.gov/books/NBK7986/</ref>.  
[[Penicillin|Penicillin]] [[Inhibits|inhibits]] the effect of peptidoglycan in&nbsp;bacteria by binding to [[Serine|serine]] in the enzyme [[Glycopeptide transpeptidase|glycopeptide transpeptidase]].&nbsp;As a result,&nbsp;it&nbsp;can no longer catalyse the formation of cross-links.&nbsp;The enzyme is irreversibly inhibitted which therefore results&nbsp;in the termination of bacterial growth<ref>http://www.ncbi.nlm.nih.gov/books/NBK7986/</ref>.  


Penicillin&nbsp;inhibits the transpeptidase linking together the polysaccheride chains and cells become osmotically sensitive and burst.
Penicillin&nbsp;inhibits the transpeptidase linking together the polysaccharide chains and cells become osmotically sensitive and burst.  


=== References  ===
=== References  ===


<references />
<references />

Revision as of 17:57, 1 December 2017

Peptidoglycan is found in both Gram-negative and Gram-positive bacteria. It is present in larger amounts in Gram-positive bacteria as it appears as a multimolecular layer and can be found in association with additional compounds. In Gram-negative bacteria, it is found in either 1 or 2 layers between the inner and outer membrane [1]

Peptidoglycan is a macromolecule made up of alternating residues of N-acetyl-β-D-glucosamine (NAG) and N-acetylmuramic acid (NAM) joined together by a glycosidic bond[2]. There is then a pentapeptide attatched to the NAM amino acid which forms cross-links with other polysaccharide chains forming a 3D mesh-like layer. These cross-links are formed using the enzyme glycopeptide transpeptidase and provide peptidoglycan with stability. This stability allows it to provide mechanical support and prevent osmotic lysis from occurring in bacteria [3].

Penicillin inhibits the effect of peptidoglycan in bacteria by binding to serine in the enzyme glycopeptide transpeptidase. As a result, it can no longer catalyse the formation of cross-links. The enzyme is irreversibly inhibitted which therefore results in the termination of bacterial growth[4].

Penicillin inhibits the transpeptidase linking together the polysaccharide chains and cells become osmotically sensitive and burst.

References