Sandbox Reserved 1066: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 13: | Line 13: | ||
= 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="Our Paper">PMID: PMC2793005</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]] | ||
| Line 40: | Line 42: | ||
== Active Site == | == Active Site == | ||
The active site on FadD13 is composed of two conserved regions, one of which serves as the binding site for ATP and the other for CoA. The adenine of ATP is bound to a group of <scene name='69/694232/Adenine_binding_group/2'>six amino acids (300-305)</scene> that is structurally identically to other acyl-CoA synthetases. <ref name="Our Paper"/> | The active site on FadD13 is composed of two conserved regions, one of which serves as the binding site for ATP and the other for CoA. The adenine of ATP is bound to a group of <scene name='69/694232/Adenine_binding_group/2'>six amino acids (300-305)</scene> that is structurally identically to other acyl-CoA synthetases. <ref name="Our Paper"/> | ||
= Disease = | = Disease = | ||
