Sandbox Reserved 1066: Difference between revisions

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= Mechanism =
= Mechanism =
[[Image:FadD13 edited image.jpg|425 px|left|thumb|Figure 1: Mechanism for the activation of fatty acids (C24-C26) by FadD13. The N terminal domain (pink) is embedded in the membrane with the arginine rich lid-loop (dark blue), while the flexile linker (black) connects the C terminal domain (green) to the rest of the enzyme. Activation requires the binding of ATP (blue) which induces structural changes that promote the binding of the fatty acid chain. Formation of an acyl-adenylate intermediate induces a 140° rotation of the C terminal domain and the binding of CoA (orange). ]]
[[Image:FadD13 edited image.jpg|425 px|left|thumb|Figure 1: Mechanism for the activation of fatty acids (C24-C26) by FadD13. The N terminal domain (pink) is embedded in the membrane with the arginine rich lid-loop (dark blue), while the flexile linker (black) connects the C terminal domain (green) to the rest of the enzyme. Activation requires the binding of ATP (blue) which induces structural changes that promote the binding of the fatty acid chain. Formation of an acyl-adenylate intermediate induces a 140° rotation of the C terminal domain and the binding of CoA (orange). ]]
<scene name='69/694233/Lys_487/2'>Lys 487</scene> results in a 95% loss of function of FadD13. <ref name="residue paper">PMID: 20027301</ref>


[[Image:acyl coa synthetase.jpg|425 px|left|thumb|Figure 2: Representation of the two-step reaction catalyzed by FadD13]]
[[Image:acyl coa synthetase.jpg|425 px|left|thumb|Figure 2: Representation of the two-step reaction catalyzed by FadD13]]