User:Jacob Holt/Sandbox 1

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== Introduction==
== Introduction==
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Stearyol CoA Desaturase (SCD1) functions as a lipogenic enzyme which is essential for fatty acid metabolism<ref name=”Bai”>PMID: 26098370 </ref>. SCD1 desaturates the sigma bond, within the 18-carbon acyl-CoA ligand, that attaches carbons 9 and 10 <ref name=”Bai” />. The desaturated ligand is used in the synthesis of [https://en.wikipedia.org/wiki/Cholesteryl_ester cholesteryl esters] and [https://en.wikipedia.org/wiki/Triglyceride triglycerides]. The exact origin of SCD1 is unknown. Current studies have used mouse SCD to determine the structure and function of the enzyme. The metal ions within the structure of SCD1 were determined by [https://en.wikipedia.org/wiki/X-ray_fluorescence X-Ray Flourescense]. The structure of the ligand before the reaction takes place and how it interacts with the enzyme was determined by using [https://en.wikipedia.org/wiki/Zinc zinc] as the metal ions which inhibits the enzymes activity<ref name=”Bai” />. The structure of the ligand post reaction was determined by using [hhttps://en.wikipedia.org/wiki/Iron iron] as the metal ions which allowed the enzyme to be active and complete the reaction. SCD1 is a [https://en.wikipedia.org/wiki/Transmembrane_protein transmembrane protein title] with 4 helices within the membrane, and 8 helices in cytoplasm. This protein acquires electrons via an electron transport chain which includes [https://en.wikipedia.org/wiki/Cytochrome_b5_reductase cytochrome B5 reductase] and [https://en.wikipedia.org/wiki/Cytochrome_b5 cytochrome B5]. The electrons are transferred via a ternary complex and accepted by SCD1 by the iron metal ions. SCD1 has 8 helices that are hydrophobic, 4 helices that are hydrophilic, and 3 helices that are amphipathic<ref name=”Bai” />
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Stearyol CoA Desaturase (SCD1) functions as a lipogenic enzyme which is essential for fatty acid metabolism<ref name="Bai">PMID: 26098370 </ref>. SCD1 desaturates the sigma bond, within the 18-carbon acyl-CoA ligand, that attaches carbons 9 and 10 <ref name="Bai" />. The desaturated ligand is used in the synthesis of [https://en.wikipedia.org/wiki/Cholesteryl_ester cholesteryl esters] and [https://en.wikipedia.org/wiki/Triglyceride triglycerides]<ref name="Paton">PMID: 19066317 </ref>. The exact origin of SCD1 is unknown. Current studies have used mouse SCD to determine the structure and function of the enzyme<ref name="Shen">PMID: 32470559 </ref>. The metal ions within the structure of SCD1 were determined by [https://en.wikipedia.org/wiki/X-ray_fluorescence X-Ray Flourescense]. The structure of the ligand before the reaction takes place and how it interacts with the enzyme was determined by using [https://en.wikipedia.org/wiki/Zinc zinc] as the metal ions which inhibits the enzymes activity<ref name="Bai" />. The structure of the ligand post reaction was determined by using [hhttps://en.wikipedia.org/wiki/Iron iron] as the metal ions which allowed the enzyme to be active and complete the reaction<ref name="Shen" />. SCD1 is a [https://en.wikipedia.org/wiki/Transmembrane_protein transmembrane protein title] with 4 helices within the membrane, and 8 helices in cytoplasm. This protein acquires electrons via an electron transport chain which includes [https://en.wikipedia.org/wiki/Cytochrome_b5_reductase cytochrome B5 reductase] and [https://en.wikipedia.org/wiki/Cytochrome_b5 cytochrome B5]<ref name="Shen" />. The electrons are transferred via a ternary complex and accepted by SCD1 by the iron metal ions<ref name="Shen" />. SCD1 has 8 helices that are hydrophobic, 4 helices that are hydrophilic, and 3 helices that are amphipathic<ref name="Bai" /><ref name="Shen" />.
== Biological Relevance ==
== Biological Relevance ==
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Position within membrane
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The primary job of SCD1 in the body is to catalyze the biosynthesis of monounsaturated fatty acids (MUFAs) via saturated [https://en.wikipedia.org/wiki/Acyl-CoA Acyl-CoAs] with an acyl chain length of 14-19 carbons<ref name="Paton" /><ref name="Shen" />. Variations of the monounsaturated fatty acids function as precursors for the biosynthesis of [https://en.wikipedia.org/wiki/Phospholipid phospholipids], cholesterol esters, and triglycerides; therefore, SCD1 is a promising candidate for drug targeting1. Absence or a deficit of SCD1 in the body is associated with obesity and insulin resistance which is a main cause of [https://en.wikipedia.org/wiki/Type_2_diabetes type II diabetes]<ref name="Shen" />. Cancer sites in the body tend to show a much higher expression rate of SCD13. Focusing on SCD1 as a drug target could lead to advancements in treatment of obesity, diabetes, and other metabolic diseases<ref name="Bai" />.
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<scene name='87/877556/Diiron_center/1'>Dizinc Center</scene>
<scene name='87/877556/Diiron_center/1'>Dizinc Center</scene>
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[http://https://en.wikipedia.org/wiki/Fatty_acid_desaturase Desaturase Enzyme]
[http://https://en.wikipedia.org/wiki/Fatty_acid_desaturase Desaturase Enzyme]
<scene name='87/877552/140-160_amino_highlight/1'>SCD thing</scene>
<scene name='87/877552/140-160_amino_highlight/1'>SCD thing</scene>
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SCD function <ref name=”Gibson”>PMID: 32733502 </ref>
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== Disease ==
== Disease ==
== Structural highlights ==
== Structural highlights ==
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[[Image:SCD1_New.jpeg|300px|]]
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[[Image:SCD1_New.jpeg|500px|Right|]]
</StructureSection>
</StructureSection>

Revision as of 14:27, 30 March 2021

Mouse Stearoyl-CoA Desaturase-1 Structure

Mouse SCD1 Protein 4ymk

Drag the structure with the mouse to rotate

References

  1. 1.0 1.1 1.2 1.3 1.4 Bai Y, McCoy JG, Levin EJ, Sobrado P, Rajashankar KR, Fox BG, Zhou M. X-ray structure of a mammalian stearoyl-CoA desaturase. Nature. 2015 Jun 22. doi: 10.1038/nature14549. PMID:26098370 doi:http://dx.doi.org/10.1038/nature14549
  2. 2.0 2.1 Paton CM, Ntambi JM. Biochemical and physiological function of stearoyl-CoA desaturase. Am J Physiol Endocrinol Metab. 2009 Jul;297(1):E28-37. doi:, 10.1152/ajpendo.90897.2008. Epub 2008 Dec 9. PMID:19066317 doi:http://dx.doi.org/10.1152/ajpendo.90897.2008
  3. 3.0 3.1 3.2 3.3 3.4 3.5 3.6 Shen J, Wu G, Tsai AL, Zhou M. Structure and Mechanism of a Unique Diiron Center in Mammalian Stearoyl-CoA Desaturase. J Mol Biol. 2020 May 27. pii: S0022-2836(20)30367-3. doi:, 10.1016/j.jmb.2020.05.017. PMID:32470559 doi:http://dx.doi.org/10.1016/j.jmb.2020.05.017



Student Contributions

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Proteopedia Page Contributors and Editors (what is this?)

Jacob Holt

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