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Stearoyl-CoA 9-desaturase
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<h2 id="function">Function</h2> <p>Stearoyl-CoA desaturase (SCD; EC 1.14.19.1) is an iron-containing enzyme that catalyzes a rate-limiting step in the synthesis of <a href="/facts/Unsaturated_fatty_acid/87HcP11s">unsaturated fatty acids</a>. The principal product of SCD is <a href="/facts/Oleic_acid/NeVuHTbe">oleic acid</a>, which is formed by desaturation of stearic acid. The ratio of stearic acid to oleic acid has been implicated in the regulation of cell growth and differentiation through effects on cell membrane fluidity and signal transduction. </p><p>Four SCD <a href="/facts/Isoform/oWmzfg4l">isoforms</a>, Scd1 through Scd4, have been identified in mouse. In contrast, only 2 SCD isoforms, SCD1 and SCD5 (MIM 608370, Uniprot <a href="https://www.uniprot.org/uniprot/Q86SK9">Q86SK9</a>), have been identified in human. SCD1 shares about 85% amino acid identity with all 4 mouse SCD isoforms, as well as with rat Scd1 and Scd2. In contrast, SCD5 (also known as hSCD2) shares limited homology with the rodent SCDs and appears to be unique to primates.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a><a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a><a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a><a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> </p><p>SCD-1 is an important metabolic control point. Inhibition of its expression may enhance the treatment of a host of <a href="/facts/Metabolic_disorder/mXnwRURT">metabolic diseases</a>.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> One of the unanswered questions is that SCD remains a highly regulated enzyme, even though oleate is readily available, as it is an abundant monounsaturated fatty acid in dietary fat. </p><p>It <a href="/facts/Catalysis/LPBS7TQC">catalyzes</a> the <a href="/facts/Chemical_reaction/GpqWlKrz">chemical reaction</a> </p> stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ ⇌ {\displaystyle \rightleftharpoons } oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O <p>The 4 <a href="/facts/Substrate_(biochemistry)/6MnaV19h">substrates</a> of this enzyme are <a href="/facts/Stearoyl-CoA/wNh77Pqt">stearoyl-CoA</a>, <a href="/facts/Ferrocytochrome_b5/cG3Jh8Y6">ferrocytochrome b5</a>, <a href="/facts/Oxygen/acyn6o8r">O2</a>, and <a href="/facts/Hydrogen_ion/6UbSyoz4">H+</a>, whereas its 3 <a href="/facts/Product_(chemistry)/8uCoDUdv">products</a> are oleoyl-CoA, <a href="/facts/Ferricytochrome_b5/cG3Jh8Y6">ferricytochrome b5</a>, and <a href="/facts/Water/0lkXnJPK">H2O</a>. </p> <h2 id="structure">Structure</h2> <p>The enzyme's structure is key to its function. SCD-1 consists of four transmembrane domains. Both the <a href="/facts/N-terminus/yKYpuaBJ">amino</a> and <a href="/facts/C-terminus/ws4scHgT">carboxyl terminus</a> and eight catalytically important <a href="/facts/Histidine/le7781NF">histidine</a> regions, which collectively bind iron within the catalytic center of the enzyme, lie in the cytosol region. The five cysteines in SCD-1 are located within the lumen of the <a href="/facts/Endoplasmic_reticulum/DVbLA7GE">endoplasmic reticulum</a>.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> </p><p>The <a href="/facts/Binding_site/gd9r9Rw7">substrate binding site</a> is long, thin and <a href="/facts/Hydrophobic/Ifya0CXQ">hydrophobic</a> and kinks the substrate tail at the location where the di-iron <a href="/facts/Catalytic_centre/u9ua7rGu">catalytic centre</a> introduces the double bond.<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> </p> <p>The literature suggests that the enzyme accomplishes the desaturation reaction by removing the first hydrogen at C9 position and then the second hydrogen from the C-10 position.<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> Because the C-9 and C-10 are positioned close to the iron-containing center of the enzyme, this mechanism is hypothesized to be specific for the position at which the double bond is formed. </p> <h2 id="role-in-human-disease">Role in human disease</h2> <p>Monounsaturated fatty acids, the products of SCD-1 catalyzed reactions, can serve as <a href="/facts/Substrate_(chemistry)/6MnaV19h">substrates</a> for the synthesis of various kinds of lipids, including phospholipids, triglycerides, and can also be used as mediators in <a href="/facts/Signal_transduction/1bs0Me6w">signal transduction</a> and differentiation.<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> Because MUFAs are heavily utilized in cellular processes, variation in SCD activity in mammals is expected to influence physiological variables, including <a href="/facts/Cellular_differentiation/bCVqUG7w">cellular differentiation</a>, insulin sensitivity, metabolic syndrome, atherosclerosis, <a href="/facts/Cancer/PVW6n1D0">cancer</a>, and <a href="/facts/Obesity/RBF9y5Vl">obesity</a>. SCD-1 deficiency results in reduced <a href="/facts/Adipose_tissue/PxxedB6e">adiposity</a>, increased insulin sensitivity, and resistance to diet-induced obesity.<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> </p><p>Under non-fasting conditions, SCD-1 mRNA is highly expressed in <a href="/facts/White_adipose_tissue/VGUkQNv6">white adipose tissue</a>, <a href="/facts/Brown_adipose_tissue/ut8P9TLS">brown adipose tissue</a>, and the <a href="/facts/Harderian_gland/nuU8w9Tt">Harderian gland</a>.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a> SCD-1 expression is significantly increased in liver tissue and heart in response to a high-carbohydrate diet, whereas SCD-2 expression is observed in brain tissue and induced during the <a href="/facts/Myelination/DKgJB8s8">neonatal myelination</a>.<a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a> Diets high in high-saturated as well as monounsaturated-fat can also increase SCD-1 expression, although not to the extent of the lipogenic effect of a high-carb diet.<a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a> </p><p>Elevated expression levels of SCD1 is found to be correlated with obesity <a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a> and tumor malignancy.<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a> It is believed that tumor cells obtain most part of their requirement for fatty acids by de novo synthesis. This phenomenon depends on increased expression of fatty acid biosynthetic enzymes that produce required fatty acids in large quantities.<a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a> Mice that were fed a high-carbohydrate diet had an induced expression of the liver SCD-1 gene and other lipogenic genes through an insulin-mediated <a href="/facts/Sterol_regulatory_element-binding_protein_1/hVAr7UPW">SREBP-1c</a>-dependent mechanism. Activation of SREBP-1c results in upregulated synthesis of MUFAs and liver <a href="/facts/Triglyceride/BQmjv4A0">triglycerides</a>. SCD-1 knockout mice did not increase de novo <a href="/facts/Lipogenesis/ur2r9sbV">lipogenesis</a> but created an abundance of cholesterol esters.<a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a> </p><p>SCD1 function has also been shown to be involved in germ cell determination,<a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a> adipose tissue specification, liver cell differentiation<a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a> and cardiac development.<a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a> </p><p>The human SCD-1 gene structure and regulation is very similar to that of mouse SCD-1. Overexpression of SCD-1 in humans may be involved in the development of <a href="/facts/Hypertriglyceridemia/ztlqAVgG">hypertriglyceridemia</a>, <a href="/facts/Atherosclerosis/WIS8QQ6v">atherosclerosis</a>, and <a href="/facts/Diabetes_mellitus/2xeHXbsI">diabetes</a>.<a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a> One study showed that SCD-1 activity was associated with inherited <a href="/facts/Hyperlipidemia/3QNcXN9l">hyperlipidemia</a>. SCD-1 deficiency has also been shown to reduce ceramide synthesis by downregulating serine palmitoyltransferase. This consequently increases the rate of <a href="/facts/Beta_oxidation/mbwIMN7D">beta-oxidation</a> in skeletal muscle.<a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a> </p><p>In carbohydrate metabolism studies, knockout SCD-1 mice show increased <a href="/facts/Insulin_sensitivity/cz6oFqke">insulin sensitivity</a>. Oleate is a major constituent of membrane phospholipids and membrane fluidity is influenced by the ratio of saturated to monounsaturated fatty acids.<a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a> One proposed mechanism is that an increase in cell membrane fluidity, consisting largely of lipid, activates the <a href="/facts/Insulin_receptor/PCEbQj6k">insulin receptor</a>. A decrease in MUFA content of the membrane phospholipids in the SCD-1−/− mice is offset by an increase in polyunsaturated fatty acids, effectively increasing membrane fluidity due to the introduction of more double bonds in the fatty acyl chain.<a class="footnote-ref" id="fnref:30" href="#fn:30"><sup>30</sup></a> </p> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/Cyclopropene_acid/FaUbHBgI">Cyclopropene acid</a></li> <li><a href="/facts/Fatty_acid_desaturase/edjFHcuj">Fatty acid desaturase</a></li> <li><a href="/facts/Fatty_acid_synthesis/Cl17j9xE">Fatty acid synthesis</a></li></ul> <h2 id="bibliography">Bibliography</h2> <ul><li>FULCO AJ, BLOCH K (1964). <a href="https://doi.org/10.1016%2FS0021-9258%2818%2991378-5">"Cofactor Requirements for the Formation of Delta-9-Unsaturated Fatty Acids in Mycobacterium Phlei"</a>. <i>J. Biol. Chem</i>. 239 (4): 993–7. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0021-9258%2818%2991378-5">10.1016/S0021-9258(18)91378-5</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/14167617">14167617</a>.</li> <li>Oshino N, Imai Y, Sato R (1966). "Electron-transfer mechanism associated with fatty acid desaturation catalyzed by liver microsomes". <i>Biochim. Biophys. Acta</i>. 128 (1): 13–27. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0926-6593%2866%2990137-8">10.1016/0926-6593(66)90137-8</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/4382040">4382040</a>.</li> <li>Oshino N, Imai Y, Sato R (January 1971). "A function of cytochrome b5 in fatty acid desaturation by rat liver microsomes". <i>J. Biochem</i>. 69 (1). Tokyo: 155–67. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Foxfordjournals.jbchem.a129444">10.1093/oxfordjournals.jbchem.a129444</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/5543646">5543646</a>.</li> <li>Strittmatter P, Spatz L, Corcoran D, Rogers MJ, Setlow B, Redline R (1974). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC433928">"Purification and properties of rat liver microsomal stearyl coenzyme A desaturase"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. 71 (11): 4565–9. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.71.11.4565">10.1073/pnas.71.11.4565</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC433928">433928</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/4373719">4373719</a>.</li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Mziaut H, Korza G, Ozols J (Aug 2000). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC16790">"The N terminus of microsomal Δ 9 stearoyl-CoA desaturase contains the sequence determinant for its rapid degradation"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 97 (16): 8883–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.97.16.8883">10.1073/pnas.97.16.8883</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC16790">16790</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10922050">10922050</a>.</li> <li>Samuel W, Kutty RK, Nagineni S, Gordon JS, Prouty SM, Chandraratna RA, Wiggert B (Aug 2001). <a href="https://doi.org/10.1074%2Fjbc.M103587200">"Regulation of stearoyl coenzyme A desaturase expression in human retinal pigment epithelial cells by retinoic acid"</a>. <i>The Journal of Biological Chemistry</i>. 276 (31): 28744–50. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M103587200">10.1074/jbc.M103587200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11397803">11397803</a>.</li> <li>Zhang L, Ge L, Tran T, Stenn K, Prouty SM (Jul 2001). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221940">"Isolation and characterization of the human stearoyl-CoA desaturase gene promoter: requirement of a conserved CCAAT cis-element"</a>. <i>The Biochemical Journal</i>. 357 (Pt 1): 183–93. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1042%2F0264-6021%3A3570183">10.1042/0264-6021:3570183</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221940">1221940</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11415448">11415448</a>.</li> <li>Samuel W, Nagineni CN, Kutty RK, Parks WT, Gordon JS, Prouty SM, Hooks JJ, Wiggert B (Jan 2002). <a href="https://doi.org/10.1074%2Fjbc.M108730200">"Transforming growth factor-beta regulates stearoyl coenzyme A desaturase expression through a Smad signaling pathway"</a>. <i>The Journal of Biological Chemistry</i>. 277 (1): 59–66. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M108730200">10.1074/jbc.M108730200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11677241">11677241</a>.</li> <li>Choi Y, Park Y, Storkson JM, Pariza MW, Ntambi JM (Jun 2002). "Inhibition of stearoyl-CoA desaturase activity by the cis-9,trans-11 isomer and the trans-10,cis-12 isomer of conjugated linoleic acid in MDA-MB-231 and MCF-7 human breast cancer cells". <i>Biochemical and Biophysical Research Communications</i>. 294 (4): 785–90. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0006-291X%2802%2900554-5">10.1016/S0006-291X(02)00554-5</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12061775">12061775</a>.</li> <li>Attie AD, Krauss RM, Gray-Keller MP, Brownlie A, Miyazaki M, Kastelein JJ, Lusis AJ, Stalenhoef AF, Stoehr JP, Hayden MR, Ntambi JM (Nov 2002). <a href="https://doi.org/10.1194%2Fjlr.M200189-JLR200">"Relationship between stearoyl-CoA desaturase activity and plasma triglycerides in human and mouse hypertriglyceridemia"</a>. <i>Journal of Lipid Research</i>. 43 (11): 1899–907. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1194%2Fjlr.M200189-JLR200">10.1194/jlr.M200189-JLR200</a>. <a href="/facts/Hdl_(identifier)/rdebSxmC">hdl</a>:<a href="https://hdl.handle.net/2066%2F185468">2066/185468</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12401889">12401889</a>.</li> <li>Cohen P, Ntambi JM, Friedman JM (Dec 2003). "Stearoyl-CoA desaturase-1 and the metabolic syndrome". <i>Current Drug Targets. Immune, Endocrine and Metabolic Disorders</i>. 3 (4): 271–80. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.2174%2F1568008033340117">10.2174/1568008033340117</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/14683458">14683458</a>.</li> <li>Shiwaku K, Hashimoto M, Kitajima K, Nogi A, Anuurad E, Enkhmaa B, Kim JM, Kim IS, Lee SK, Oyunsuren T, Shido O, Yamane Y (May 2004). <a href="https://doi.org/10.1194%2Fjlr.M300483-JLR200">"Triglyceride levels are ethnic-specifically associated with an index of stearoyl-CoA desaturase activity and n-3 PUFA levels in Asians"</a>. <i>Journal of Lipid Research</i>. 45 (5): 914–22. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1194%2Fjlr.M300483-JLR200">10.1194/jlr.M300483-JLR200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/14967817">14967817</a>.</li> <li>Wang Y, Kurdi-Haidar B, Oram JF (May 2004). <a href="https://doi.org/10.1194%2Fjlr.M400011-JLR200">"LXR-mediated activation of macrophage stearoyl-CoA desaturase generates unsaturated fatty acids that destabilize ABCA1"</a>. <i>Journal of Lipid Research</i>. 45 (5): 972–80. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1194%2Fjlr.M400011-JLR200">10.1194/jlr.M400011-JLR200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/14967823">14967823</a>.</li> <li>Rahman SM, Dobrzyn A, Dobrzyn P, Lee SH, Miyazaki M, Ntambi JM (Sep 2003). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC196935">"Stearoyl-CoA desaturase 1 deficiency elevates insulin-signaling components and down-regulates protein-tyrosine phosphatase 1B in muscle"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 100 (19): 11110–5. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/2003PNAS..10011110R">2003PNAS..10011110R</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.1934571100">10.1073/pnas.1934571100</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC196935">196935</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12960377">12960377</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li><a href="https://meshb.nlm.nih.gov/record/ui?name=Stearoyl-CoA+Desaturase">Stearoyl-CoA+Desaturase</a> at the U.S. National Library of Medicine <a href="/facts/Medical_Subject_Headings/C57g2JuF">Medical Subject Headings</a> (MeSH)</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Paton CM, Ntambi JM (2017-03-08). "Biochemical and physiological function of stearoyl-CoA desaturase". American Journal of Physiology. Endocrinology and Metabolism. 297 (1): E28 – E37. doi:10.1152/ajpendo.90897.2008. ISSN 0193-1849. PMC 2711665. PMID 19066317. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2711665" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2711665</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>"Entrez Gene: Stearoyl-CoA desaturase (delta-9-desaturase)". Retrieved 2011-09-29. <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&list_uids=6319" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&list_uids=6319</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>"SCD5 stearoyl-CoA desaturase 5 [Homo sapiens (human) ]". Gene. National Library of Medicine. 5 March 2024. Gene ID No. 79966. Retrieved 22 March 2024. <a href="https://www.ncbi.nlm.nih.gov/gene/79966" target="_blank">https://www.ncbi.nlm.nih.gov/gene/79966</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Igal RA, Sinner DI (2021). "Stearoyl-CoA desaturase 5 (SCD5), a Δ-9 fatty acyl desaturase in search of a function". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1866 (1). PMC 8533680. PMID 33049404. Art. No. 158840. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8533680" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8533680</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Paton CM, Ntambi JM (2017-03-08). "Biochemical and physiological function of stearoyl-CoA desaturase". American Journal of Physiology. Endocrinology and Metabolism. 297 (1): E28 – E37. doi:10.1152/ajpendo.90897.2008. ISSN 0193-1849. PMC 2711665. 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