Sandbox Reserved 1066: Difference between revisions

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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 both the activation of fatty acids and other hydrophobic substrates in addition to the transport of these lipids into the cell. However, substrates longer than the enzyme itself, like these very-long-chain fatty acids, pose and interesting structural dilemma to the enzyme. 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 both the activation of fatty acids and other hydrophobic substrates in addition to the transport of these lipids into the cell. However, substrates longer than the enzyme itself, like these very-long-chain fatty acids, pose and interesting structural dilemma to the enzyme. In order for FadD13 to accommodate these very long substrates, it differs structurally in that it exists as a peripheral protein on the inside of the cell membrane. This feature is key to 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>