Sandbox Reserved 1066: Difference between revisions
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== 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 FadD13 active site is composed of positively charged regions which account for the attraction and binding of hydrophobic substrates to this region. 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"/> | ||
Mutational studies showed that high conserved residue in the C-terminal region, <scene name='69/694233/Lys_487/2'>Lysine 487</scene>, resulted in a 95% loss of function of FadD13 and is thought to be involved in the orientation of the substrates to form the adenylate intermediate.<ref name="residue paper">PMID: 20027301</ref> Additionally, Serine 404 was hypothesized to be involved in the binding of Coenzyme A which may only occur once this region incurs a 140 degree rotational change.<ref name="Our Paper"/><ref name="residue paper"/> | Mutational studies showed that high conserved residue in the C-terminal region, <scene name='69/694233/Lys_487/2'>Lysine 487</scene>, resulted in a 95% loss of function of FadD13 and is thought to be involved in the orientation of the substrates to form the adenylate intermediate.<ref name="residue paper">PMID: 20027301</ref> Additionally, Serine 404 was hypothesized to be involved in the binding of Coenzyme A which may only occur once this region incurs a 140 degree rotational change.<ref name="Our Paper"/><ref name="residue paper"/> | ||
