Life is divided into three distinct groups: Eukaria, Bacteria and Archaea. Out of these three domains the last two had been characterized almost as equal . However with the advent of DNA sequencing, it has been widely shown that Bacteria and Archaea are phylogenetically distant organisms. In fact, some theories suggest that they have not even evolved from a common ancestor but most likely the result of convergent evolution (Ganesh Ram R. Visweswaran & Bauke W. Dijkstra. 2011). One important distinction between the two domains is their cell wall. Although, structurally and functionally similar fundamental differences lie behind their chemistry that provide scientist with good grounds to make a comparable distinction between the two domains.
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The rest of Archaea usually are endowed with only an S-layer. Archaea also have a plasma membrane made of phospolipids. However this membrane differes radically from the Bacteria 's membrane by their chemical linkages and arrangement. Bacterial membranes arrange in two sheets of membrane called a bilayer while some Archaea arrange in monolayers. This structure give hyperthermopile as methanogenic Archaea a biological advantage over Bacteria to withstand high temperatures. (Terry J. Beveridge and Susanne Schultze-Lam …show more content…
Thomas Pitzer. Jose Alberte. 2012). Methanogenic Archaea are one of these extremophiles most specific hydrothermophiles. Methanogenic Archaea are known to possess pseudomurein/pseudopeptidoglycan a similar wall to murein but with fundamental molecular differences. (O. Kandlera. H. Konigb. 1998). This type of Archaea are also known to produce as a by product methane and they also live on extreme hydrothermal enviroment that lack oxygen. Pseudomurein is made of N-acetyltalosaminuronic acid
( NAT) and N-acetyl-D-glucosamine (NAG) while murein is made of N-acetyl-D-glucosamine but instead of NAT it has N- acetylmuramic acid. SHOCKMAN. DANEO-MOORE. R.KARIYAMA. O. MASSIDDA. (1996). Although their structure and even function have certain similarities ( protection and structure) their biosynthetic pathways differ. One important disticntion between the two wall are their cell binding domains. As mentioned earlier Bacterial binding domain provide hydrolase enzymes good anchorage to do their respective jobs. However, so far there is no evidence of any hydrolase that can bind to the Archaeal wall and digest their glycosidic bonds. (Ganesh Ram R. Visweswaran & Bauke W. Dijkstra. 2011) The reason for this might be the fact that methanogenic Archea binding sites differ at a molecular level from E.choli. Because enzymes are extremely specific
The rest of Archaea usually are endowed with only an S-layer. Archaea also have a plasma membrane made of phospolipids. However this membrane differes radically from the Bacteria 's membrane by their chemical linkages and arrangement. Bacterial membranes arrange in two sheets of membrane called a bilayer while some Archaea arrange in monolayers. This structure give hyperthermopile as methanogenic Archaea a biological advantage over Bacteria to withstand high temperatures. (Terry J. Beveridge and Susanne Schultze-Lam …show more content…
Thomas Pitzer. Jose Alberte. 2012). Methanogenic Archaea are one of these extremophiles most specific hydrothermophiles. Methanogenic Archaea are known to possess pseudomurein/pseudopeptidoglycan a similar wall to murein but with fundamental molecular differences. (O. Kandlera. H. Konigb. 1998). This type of Archaea are also known to produce as a by product methane and they also live on extreme hydrothermal enviroment that lack oxygen. Pseudomurein is made of N-acetyltalosaminuronic acid
( NAT) and N-acetyl-D-glucosamine (NAG) while murein is made of N-acetyl-D-glucosamine but instead of NAT it has N- acetylmuramic acid. SHOCKMAN. DANEO-MOORE. R.KARIYAMA. O. MASSIDDA. (1996). Although their structure and even function have certain similarities ( protection and structure) their biosynthetic pathways differ. One important disticntion between the two wall are their cell binding domains. As mentioned earlier Bacterial binding domain provide hydrolase enzymes good anchorage to do their respective jobs. However, so far there is no evidence of any hydrolase that can bind to the Archaeal wall and digest their glycosidic bonds. (Ganesh Ram R. Visweswaran & Bauke W. Dijkstra. 2011) The reason for this might be the fact that methanogenic Archea binding sites differ at a molecular level from E.choli. Because enzymes are extremely specific