Isocitrate dehydrogenase: Difference between revisions
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=='''Mechanism'''== | =='''Mechanism'''== | ||
The mechanism described is for porcine isocitrate dehydrogenase because is is better understood than the human mechanism. The alcohol group off the alpha-carbon is deprotonated by the Tyr residue. The electrons pust to the oxygen atom to form a double bond (keytone). The remaining alpha carbon hydrogen is removed using NAD+/NADP+ as an electron accepting cofactor. A carboxyl group pushes electrons down so an oxygen steals a nearby proton off a Lysine amino acid. The Tyr deprotanates the carboxylic acid resulting in electron pushing that ejects a CO2. The two negatively charged | The mechanism described is for porcine isocitrate dehydrogenase because is is better understood than the human mechanism. The alcohol group off the alpha-carbon is deprotonated by the Tyr residue. The electrons pust to the oxygen atom to form a double bond (keytone). The remaining alpha carbon hydrogen is removed using NAD+/NADP+ as an electron accepting cofactor. A carboxyl group pushes electrons down so an oxygen steals a nearby proton off a Lysine amino acid. The Tyr deprotanates the carboxylic acid resulting in electron pushing that ejects a CO2. The two negatively charged oxygen's on the other side of the molecule are stabilized by the Mn2+. The double bond that was formed between the alpha and beta carbon removes a proton from the Tyr residue and the oxygen returns the a keytone and the alpha-ketoglutarate is formed. This is illustrated in the figure below. | ||
<scene name='Michael_nobbe_sandbox_2/Ligand/1'>Interactive Ligand</scene> | |||
=='''References'''== | =='''References'''== | ||