User:Nicholas Bantz/Sandbox 1: Difference between revisions
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== Mechanism of Action== | == Mechanism of Action== | ||
[[Image: | [[Image:LSD_1_Chemdraw_Mech.png|700 px|right|thumb|Figure 3: Hydride transfer mechanism of LSD-1 active site via FAD cofactor.]] | ||
The mechanism of lysine demethylation is highly dependent on the presence of the <scene name='81/811089/Fadcofactor/5'>FAD cofactor</scene>. The FAD cofactor, positioned closely to the substrate lysine in the active site, acts as an oxidizing agent and initiates catalysis (Figure 3). A two-electron transfer occurs between the substrate lysine and the isoallozaxine ring of the FAD cofactor in the form of a [https://en.wikipedia.org/wiki/Hydride hydride]; the substrate lysine is oxidized and the FAD is reduced <ref name="Stavropolous"/>. The FAD cofactor forms an anion and is stabilized by the positively charged <scene name='81/811088/Lys661/3'>Lys661</scene> positioned in the catalytic pocket of the active site <ref name="Stavropolous"/>. The oxidized substrate lysine forms an iminium cation that is hydrolyzed into the carbinolamine intermediate <ref name="Stavropolous"/>. The carbinolamine intermediate readily decomposes into formaldehyde and the demethylated lysine substrate <ref name="Stavropolous"/>. | The mechanism of lysine demethylation is highly dependent on the presence of the <scene name='81/811089/Fadcofactor/5'>FAD cofactor</scene>. The FAD cofactor, positioned closely to the substrate lysine in the active site, acts as an oxidizing agent and initiates catalysis (Figure 3). A two-electron transfer occurs between the substrate lysine and the isoallozaxine ring of the FAD cofactor in the form of a [https://en.wikipedia.org/wiki/Hydride hydride]; the substrate lysine is oxidized and the FAD is reduced <ref name="Stavropolous"/>. The FAD cofactor forms an anion and is stabilized by the positively charged <scene name='81/811088/Lys661/3'>Lys661</scene> positioned in the catalytic pocket of the active site <ref name="Stavropolous"/>. The oxidized substrate lysine forms an iminium cation that is hydrolyzed into the carbinolamine intermediate <ref name="Stavropolous"/>. The carbinolamine intermediate readily decomposes into formaldehyde and the demethylated lysine substrate <ref name="Stavropolous"/>. | ||
