Sandbox Reserved 1544: Difference between revisions
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== Function == | == Function == | ||
The first reaction in β-oxidation, or fatty acid metabolism, is the catalyzation of the ester bond (C2 and C3) of the substrate Acyl-CoA.<ref name="Berg">Berg JM, Tymoczko JL, Stryer L. Biochemistry. 5th edition. New York: W H Freeman; 2002. Chapter 22, Fatty Acid Metabolism. Available from: https://www.ncbi.nlm.nih.gov/books/NBK21173/</ref> This is accomplished through '' | The first reaction in β-oxidation, or fatty acid metabolism, is the catalyzation of the ester bond (C2 and C3) of the substrate Acyl-CoA.<ref name="Berg">Berg JM, Tymoczko JL, Stryer L. Biochemistry. 5th edition. New York: W H Freeman; 2002. Chapter 22, Fatty Acid Metabolism. Available from: https://www.ncbi.nlm.nih.gov/books/NBK21173/</ref> This is accomplished through <scene name='49/491924/Cv/1'>acyl-CoA dehydrogenase</scene> and its cofactor <scene name='49/491924/Cv/3'>FAD</scene>.<ref name="Berg"/> ACDH is classified according to its length of its substrates: short (SCAD), medium (MCAD), very and very long-chain (VLCAD).<ref name="Lee"/> | ||
== Disease == | == Disease == | ||
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Acyl-CoA dehydrogenase is the first enzyme used to metabolize fatty acids.<ref name="Berg"/> | Acyl-CoA dehydrogenase is the first enzyme used to metabolize fatty acids.<ref name="Berg"/> | ||
In the first step, fatty acyl-CoA is converted to trans-Δ<sup>2</sup>-enoyl-CoA via acyl-CoA dehydrogenase with the help of FAD, releasing FADH<sub>2</sub> as a byproduct.<ref name="Berg"/> | In the first step, fatty acyl-CoA is converted to trans-Δ<sup>2</sup>-enoyl-CoA via <scene name='49/491924/Cv/1'>acyl-CoA dehydrogenase</scene> with the help of <scene name='49/491924/Cv/3'>FAD</scene>, releasing FADH<sub>2</sub> as a byproduct.<ref name="Berg"/> | ||
In the second step, trans-Δ<sup>2</sup>-enoyl-CoA is converted to 3-L-hydroxyacyl-CoA via enoyl-CoA hydratase with the help of H<sub>2</sub>O.<ref name="Berg"/> | In the second step, trans-Δ<sup>2</sup>-enoyl-CoA is converted to 3-L-hydroxyacyl-CoA via enoyl-CoA hydratase with the help of H<sub>2</sub>O.<ref name="Berg"/> | ||
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== Structural highlights == | == Structural highlights == | ||
'''1ege''' is a <scene name='49/491924/Cv/2'>4 chain structure</scene>, distinguished by the letters A, B, C, and D. Each chain is composed of the ligand FAD and Coenzyme A. | |||
'''Catalytic Residues''' | '''Catalytic Residues''' | ||
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Glu376 is the amino acid responsible for catalytic activity of the wild type.<ref name="Lee"/> | Glu376 is the amino acid responsible for catalytic activity of the wild type.<ref name="Lee"/> | ||
'''Significance of the Positions of Glutamate on the Wild Type (Glu376) and Mutant (Glu255)''' | '''Significance of the Positions of Glutamate on the <scene name='80/806430/Wildtype/1'>Wild Type</scene> (Glu376) and Mutant (Glu255)''' | ||
The distance between the donor proton and the base that attacks the donor proton affect the catalytic activity of the carboxylate base of the glutamates.<ref name="Lee"/> The distance between the proton and glutamates carboxylates are more than 4.0 A.<ref name="Lee"/> | The distance between the donor proton and the base that attacks the donor proton affect the catalytic activity of the carboxylate base of the glutamates.<ref name="Lee"/> The distance between the proton and glutamates carboxylates are more than 4.0 A.<ref name="Lee"/> | ||
