Peptidoglycan: Difference between revisions

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Peptidoglycan is found in both [[Gram-negative|Gram-negative]] and [[Gram-positive|Gram-positive]] [[Bacteria|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&nbsp;found in either 1 or 2 layers between the inner and outer membrane<ref>http://www.chem.qmul.ac.uk/iupac/misc/glycp.html#3.9</ref>.&nbsp;  
Peptidoglycan is found in both &lt;a href="Gram-negative"&gt;Gram-negative&lt;/a&gt; and &lt;a href="Gram-positive"&gt;Gram-positive&lt;/a&gt; &lt;a href="Bacteria"&gt;bacteria&lt;/a&gt;. 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&nbsp;found in either 1 or 2 layers between the inner and outer membrane<ref>http://www.chem.qmul.ac.uk/iupac/misc/glycp.html#3.9</ref>.&nbsp;  


Peptidoglycan is a&nbsp;[[Macromolecule|macromolecule]] made up of alternating [[Residues|residues]] of [[N-acetyl-β-D-glucosamine|N-acetyl-β-D-glucosamine]] (NAG)&nbsp;and [[N-acetylmuramic acid|N-acetylmuramic acid]] (NAM)&nbsp;joined together by a [[Glycosidic bond|glycosidic bond]]<ref>http://faculty.ccbcmd.edu/courses/bio141/lecguide/unit1/prostruct/cw.html</ref>. There&nbsp;is then a [[Pentapeptide|pentapeptide]]&nbsp;attatched&nbsp;to&nbsp;the NAM amino acid which forms cross-links&nbsp;with other&nbsp;polysaccharide chains&nbsp;forming a 3D mesh-like layer. These cross-links are formed using the enzyme [[Glycopeptide transpeptidase|glycopeptide transpeptidase]] and provide peptidoglycan with stability.&nbsp;This stability allows it to provide mechanical support and prevent osmotic lysis from occurring in bacteria<ref>Berg J., Tymoczko J and Stryer L. (2012) Biochemistry, 7th edition, New York: WH Freeman: pg 252</ref>.  
Peptidoglycan is a&nbsp;&lt;a href="Macromolecule"&gt;macromolecule&lt;/a&gt; made up of alternating &lt;a href="Residues"&gt;residues&lt;/a&gt; of &lt;a href="N-acetyl-β-D-glucosamine"&gt;N-acetyl-β-D-glucosamine&lt;/a&gt; (NAG)&nbsp;and &lt;a href="N-acetylmuramic acid"&gt;N-acetylmuramic acid&lt;/a&gt; (NAM)&nbsp;joined together by a &lt;a href="Glycosidic bond"&gt;glycosidic bond&lt;/a&gt;<ref>http://faculty.ccbcmd.edu/courses/bio141/lecguide/unit1/prostruct/cw.html</ref>. There&nbsp;is then a &lt;a href="Pentapeptide"&gt;pentapeptide&lt;/a&gt;&nbsp;attached&nbsp;to&nbsp;the NAM amino acid which forms cross-links&nbsp;with other&nbsp;polysaccharide chains&nbsp;forming a 3D mesh-like layer. These cross-links are formed using the enzyme &lt;a href="Glycopeptide transpeptidase"&gt;glycopeptide transpeptidase&lt;/a&gt; and provide peptidoglycan with stability.&nbsp;This stability allows it to provide mechanical support and prevent osmotic lysis from occurring in bacteria<ref>Berg J., Tymoczko J and Stryer L. (2012) Biochemistry, 7th edition, New York: WH Freeman: pg 252</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>.  
&lt;a href="Penicillin"&gt;Penicillin&lt;/a&gt; &lt;a href="Inhibits"&gt;inhibits&lt;/a&gt; the effect of peptidoglycan in&nbsp;bacteria by binding to &lt;a href="Serine"&gt;serine&lt;/a&gt; in the enzyme &lt;a href="Glycopeptide transpeptidase"&gt;glycopeptide transpeptidase&lt;/a&gt;.&nbsp;As a result,&nbsp;it&nbsp;can no longer catalyse the formation of cross-links.&nbsp;The enzyme is irreversibly inhibited 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 polysaccharide 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.  
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=== References  ===
=== References  ===


<references />
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Revision as of 16:17, 17 October 2018

Peptidoglycan is found in both <a href="Gram-negative">Gram-negative</a> and <a href="Gram-positive">Gram-positive</a> <a href="Bacteria">bacteria</a>. 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 <a href="Macromolecule">macromolecule</a> made up of alternating <a href="Residues">residues</a> of <a href="N-acetyl-β-D-glucosamine">N-acetyl-β-D-glucosamine</a> (NAG) and <a href="N-acetylmuramic acid">N-acetylmuramic acid</a> (NAM) joined together by a <a href="Glycosidic bond">glycosidic bond</a>[2]. There is then a <a href="Pentapeptide">pentapeptide</a> attached 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 <a href="Glycopeptide transpeptidase">glycopeptide transpeptidase</a> and provide peptidoglycan with stability. This stability allows it to provide mechanical support and prevent osmotic lysis from occurring in bacteria[3].

<a href="Penicillin">Penicillin</a> <a href="Inhibits">inhibits</a> the effect of peptidoglycan in bacteria by binding to <a href="Serine">serine</a> in the enzyme <a href="Glycopeptide transpeptidase">glycopeptide transpeptidase</a>. As a result, it can no longer catalyse the formation of cross-links. The enzyme is irreversibly inhibited 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

<span class="fck_mw_references" _fck_mw_customtag="true" _fck_mw_tagname="references" />