Sandbox Reserved 1066: Difference between revisions

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= Introduction =

''Mycobacterium tuberculosis'' very-long-chain fatty acyl-CoA synthetase, also known as FadD13, is unique within its class of FadD proteins in regards to its ability to house lipid substrates longer than itself. These lipid substrates are very-long-chain fatty acids between lengths C22 –C26, which is up to the maximum length tested. <ref name="Our Paper"/> The significance of theses very-long-chain fatty acids lies in their importance to mycolic acid synthesis by ''Mycobacterium tuberculosis'' ''(M. tb)''. Mycolic acids compose part of the cell wall of (M. tb) and have been found to be a key factor in virulence.

''Mycobacterium tuberculosis'' very-long-chain fatty acyl-CoA synthetase, also known as FadD13, is unique within its class of FadD proteins in regards to its ability to house lipid substrates longer than itself. Most FadD class proteins exist as integral membrane proteins involved in lipid transport into the cell. FadD13 is unique structurally in that it exists as a peripheral protein on the inside of the cell membrane.<ref name="Our Paper"/> This feature is key in the mechanistic basis for FadD13's activation and transport of fatty acids of length C24-C26 through the two step addition of [http://en.wikipedia.org/wiki/Coenzyme_A Coenzyme A](Figure 1).<ref name="Our Paper">PMID: 22560731</ref>

There are four main groups of FadD enzymes based on their ability to accommodate different length substrates: short (C2-C4), medium (C4-C12), long (C12-C22), and very long (C22-C26). <ref name="Our Paper"/> Most FadD class proteins exist as integral membrane proteins involved in lipid transport into the cell. FadD13 is unique structurally in that it exists as a peripheral protein on the inside of the cell membrane.<ref name="Our Paper"/> This feature is key in the mechanistic basis for FadD13's activation and transport of fatty acids of length C24-C26 through the two step addition of [http://en.wikipedia.org/wiki/Coenzyme_A Coenzyme A](Figure 1).<ref name="Our Paper">PMID: 22560731</ref>

Sandbox Reserved 1066: Difference between revisions

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 = Introduction =
-''Mycobacterium tuberculosis'' very-long-chain fatty acyl-CoA synthetase, also known as FadD13, is unique within its class of FadD proteins in regards to its ability to house lipid substrates longer than itself. These lipid substrates are very-long-chain fatty acids between lengths C22 –C26, which is up to the maximum length tested. <ref name="Our Paper"/> The significance of theses very-long-chain fatty acids lies in their importance to mycolic acid synthesis by ''Mycobacterium tuberculosis'' ''(M. tb)''. Mycolic acids compose part of the cell wall of (M. tb) and have been found to be a key factor in virulence.
+''Mycobacterium tuberculosis'' very-long-chain fatty acyl-CoA synthetase, also known as FadD13, is unique within its class of FadD proteins in regards to its ability to house lipid substrates longer than itself. Most FadD class proteins exist as integral membrane proteins involved in lipid transport into the cell. FadD13 is unique structurally in that it exists as a peripheral protein on the inside of the cell membrane.<ref name="Our Paper"/> This feature is key in the mechanistic basis for FadD13's activation and transport of fatty acids of length C24-C26 through the two step addition of [http://en.wikipedia.org/wiki/Coenzyme_A Coenzyme A](Figure 1).<ref name="Our Paper">PMID: 22560731</ref>
-There are four main groups of FadD enzymes based on their ability to accommodate different length substrates: short (C2-C4), medium (C4-C12), long (C12-C22), and very long (C22-C26). <ref name="Our Paper"/> Most FadD class proteins exist as integral membrane proteins involved in lipid transport into the cell. FadD13 is unique structurally in that it exists as a peripheral protein on the inside of the cell membrane.<ref name="Our Paper"/> This feature is key in the mechanistic basis for FadD13's activation and transport of fatty acids of length C24-C26 through the two step addition of [http://en.wikipedia.org/wiki/Coenzyme_A Coenzyme A](Figure 1).<ref name="Our Paper">PMID: 22560731</ref>