stearoyl-CoA 9-desaturase

File:Stearoyl-CoA desaturase-1 cut.png (black) held in a kinked conformation by SCD1's binding pocket which determines which bond is desaturated. ({{PDB|4ZYO}})]]

Stearoyl-CoA desaturase (SCD; EC 1.14.19.1) is an iron-containing enzyme that catalyzes a rate-limiting step in the synthesis of unsaturated fatty acids. The principal product of SCD is oleic acid, 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.{{citation needed|date=March 2024}}

Four SCD isoforms, Scd1 through Scd4, have been identified in mouse. In contrast, only 2 SCD isoforms, SCD1 and SCD5 (MIM 608370, Uniprot [https://www.uniprot.org/uniprot/Q86SK9 Q86SK9]), 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.{{cite web | title = Entrez Gene: Stearoyl-CoA desaturase (delta-9-desaturase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&list_uids=6319| access-date = 2011-09-29 }}{{cite journal | vauthors = Zhang L, Ge L, Parimoo S, Stenn K, Prouty SM | title = Human stearoyl-CoA desaturase: alternative transcripts generated from a single gene by usage of tandem polyadenylation sites | journal = The Biochemical Journal | volume = 340 | issue = Pt 1 | pages = 255–64 | date = May 1999 | pmid = 10229681 | pmc = 1220244 | doi=10.1042/bj3400255}}{{cite journal | vauthors = Wang J, Yu L, Schmidt RE, Su C, Huang X, Gould K, Cao G | title = Characterization of HSCD5, a novel human stearoyl-CoA desaturase unique to primates | journal = Biochemical and Biophysical Research Communications | volume = 332 | issue = 3 | pages = 735–42 | date = Jul 2005 | pmid = 15907797 | doi = 10.1016/j.bbrc.2005.05.013 }}{{Cite journal|last1=Zhang|first1=Shaobo|last2=Yang|first2=Yanzhu|last3=Shi|first3=Yuguang|date=2005-05-15|title=Characterization of human SCD2, an oligomeric desaturase with improved stability and enzyme activity by cross-linking in intact cells|journal=The Biochemical Journal|volume=388|issue=Pt 1|pages=135–142|doi=10.1042/BJ20041554|issn=1470-8728|pmc=1186701|pmid=15610069}}

SCD-1 is an important metabolic control point. Inhibition of its expression may enhance the treatment of a host of metabolic diseases.{{Cite journal|last1=Flowers|first1=Matthew T.|last2=Ntambi|first2=James M.|date=2017-03-09|title=Stearoyl-CoA Desaturase and its Relation to High-Carbohydrate Diets and Obesity|journal=Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids|volume=1791|issue=2|pages=85–91|doi=10.1016/j.bbalip.2008.12.011|issn=0006-3002|pmc=2649790|pmid=19166967}} 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.

It catalyzes the chemical reaction

:stearoyl-CoA + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ $\backslash rightleftharpoons$ oleoyl-CoA + 2 ferricytochrome b₅ + 2 H₂O

The 4 substrates of this enzyme are stearoyl-CoA, ferrocytochrome b5, O₂, and H⁺, whereas its 3 products are oleoyl-CoA, ferricytochrome b5, and H₂O.

The enzyme's structure is key to its function. SCD-1 consists of four transmembrane domains. Both the amino and carboxyl terminus and eight catalytically important histidine 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 endoplasmic reticulum.{{Cite journal|last1=Bai|first1=Yonghong|last2=McCoy|first2=Jason G.|last3=Levin|first3=Elena J.|last4=Sobrado|first4=Pablo|last5=Rajashankar|first5=Kanagalaghatta R.|last6=Fox|first6=Brian G.|last7=Zhou|first7=Ming|date=2015-08-13|title=X-ray structure of a mammalian stearoyl-CoA desaturase|journal=Nature|language=en|volume=524|issue=7564|pages=252–256|doi=10.1038/nature14549|issn=0028-0836|pmc=4689147|pmid=26098370|bibcode=2015Natur.524..252B}}

The substrate binding site is long, thin and hydrophobic and kinks the substrate tail at the location where the di-iron catalytic centre introduces the double bond.{{cite journal|last1=Wang|first1=Hui|last2=Klein|first2=Michael G|last3=Zou|first3=Hua|last4=Lane|first4=Weston|last5=Snell|first5=Gyorgy|last6=Levin|first6=Irena|last7=Li|first7=Ke|last8=Sang|first8=Bi-Ching|title=Crystal structure of human stearoyl–coenzyme A desaturase in complex with substrate|journal=Nature Structural & Molecular Biology|date=22 June 2015|volume=22|issue=7|pages=581–585|doi=10.1038/nsmb.3049|pmid=26098317|s2cid=205523900}}

File:Stearoyl-CoA desaturase crystal structure.png with the major ligand, stearyl-CoA (magenta), docked to the active site.{{citation needed|reason=The claim, that SCD-1 is active as a dimer, needs a reference to a reliable source.|date=June 2024}} ({{PDB|4YMK}})]]

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.{{Cite journal|last1=Nagai|first1=J.|last2=Bloch|first2=Konrad|date=1965-09-01|title=Synthesis of Oleic Acid by Euglena gracilis|url=http://www.jbc.org/content/240/9/PC3702|journal=Journal of Biological Chemistry|language=en|volume=240|issue=9|pages=PC3702–PC3703|doi=10.1016/S0021-9258(18)97206-6|issn=0021-9258|pmid=5835952|doi-access=free}} 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.

Monounsaturated fatty acids, the products of SCD-1 catalyzed reactions, can serve as substrates for the synthesis of various kinds of lipids, including phospholipids, triglycerides, and can also be used as mediators in signal transduction and differentiation.{{Cite journal|last1=Miyazaki|first1=Makoto|last2=Ntambi|first2=James M.|date=2003-02-01|title=Role of stearoyl-coenzyme A desaturase in lipid metabolism|journal=Prostaglandins, Leukotrienes, and Essential Fatty Acids|volume=68|issue=2|pages=113–121|issn=0952-3278|pmid=12538075|doi=10.1016/s0952-3278(02)00261-2}} Because MUFAs are heavily utilized in cellular processes, variation in SCD activity in mammals is expected to influence physiological variables, including cellular differentiation, insulin sensitivity, metabolic syndrome, atherosclerosis, cancer, and obesity. SCD-1 deficiency results in reduced adiposity, increased insulin sensitivity, and resistance to diet-induced obesity.{{Cite journal|last1=Flowers|first1=Matthew T.|last2=Ntambi|first2=James M.|date=2017-03-09|title=Role of stearoyl-coenzyme A desaturase in regulating lipid metabolism|journal=Current Opinion in Lipidology|volume=19|issue=3|pages=248–256|doi=10.1097/MOL.0b013e3282f9b54d|issn=0957-9672|pmc=4201499|pmid=18460915}}

Under non-fasting conditions, SCD-1 mRNA is highly expressed in white adipose tissue, brown adipose tissue, and the Harderian gland.{{Cite journal|last1=Miyazaki|first1=Makoto|last2=Dobrzyn|first2=Agnieszka|last3=Elias|first3=Peter M.|last4=Ntambi|first4=James M.|date=2005-08-30|title=Stearoyl-CoA desaturase-2 gene expression is required for lipid synthesis during early skin and liver development|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=102|issue=35|pages=12501–12506|doi=10.1073/pnas.0503132102|issn=0027-8424|pmc=1194914|pmid=16118274|bibcode=2005PNAS..10212501M|doi-access=free}} 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 neonatal myelination.{{Cite journal|last1=Miyazaki|first1=Makoto|last2=Jacobson|first2=Mark J.|last3=Man|first3=Weng Chi|last4=Cohen|first4=Paul|last5=Asilmaz|first5=Esra|last6=Friedman|first6=Jeffrey M.|last7=Ntambi|first7=James M.|date=2003-09-05|title=Identification and characterization of murine SCD4, a novel heart-specific stearoyl-CoA desaturase isoform regulated by leptin and dietary factors|journal=The Journal of Biological Chemistry|volume=278|issue=36|pages=33904–33911|doi=10.1074/jbc.M304724200 |doi-access=free |issn=0021-9258|pmid=12815040}} 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.{{Cite journal|last1=Yue|first1=Liduo|last2=Ye|first2=Fei|last3=Gui|first3=Chunshan|last4=Luo|first4=Haibin|last5=Cai|first5=Jianhua|last6=Shen|first6=Jianhua|last7=Chen|first7=Kaixian|last8=Shen|first8=Xu|last9=Jiang|first9=Hualiang|date=2017-03-09|title=Ligand-binding regulation of LXR/RXR and LXR/PPAR heterodimerizations: SPR technology-based kinetic analysis correlated with molecular dynamics simulation|journal=Protein Science|volume=14|issue=3|pages=812–822|doi=10.1110/ps.04951405|issn=0961-8368|pmc=2279270|pmid=15722453}}

Elevated expression levels of SCD1 is found to be correlated with obesity {{cite journal | vauthors = Hulver MW, Berggren JR, Carper MJ, Miyazaki M, Ntambi JM, Hoffman EP, Thyfault JP, Stevens R, Dohm GL, Houmard JA, Muoio DM | author-link11=Deborah Muoio|title = Elevated stearoyl-CoA desaturase-1 expression in skeletal muscle contributes to abnormal fatty acid partitioning in obese humans | journal = Cell Metabolism | volume = 2 | issue = 4 | pages = 251–61 | date = Oct 2005 | pmid = 16213227 | pmc = 4285571| doi = 10.1016/j.cmet.2005.09.002 }} and tumor malignancy.{{cite journal | vauthors = Ide Y, Waki M, Hayasaka T, Nishio T, Morita Y, Tanaka H, Sasaki T, Koizumi K, Matsunuma R, Hosokawa Y, Ogura H, Shiiya N, Setou M | title = Human breast cancer tissues contain abundant phosphatidylcholine(36:1) with high stearoyl-CoA desaturase-1 expression | journal = PLOS ONE | volume = 8 | issue = 4 | pages = e61204 | year = 2013 | pmid = 23613812 | pmc = 3629004 | doi = 10.1371/journal.pone.0061204 | bibcode = 2013PLoSO...861204I | doi-access = free }} 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.{{cite journal | vauthors = Mohammadzadeh F, Mosayebi G, Montazeri V, Darabi M, Fayezi S, Shaaker M, Rahmati M, Baradaran B, Mehdizadeh A, Darabi M | title = Fatty Acid Composition of Tissue Cultured Breast Carcinoma and the Effect of Stearoyl-CoA Desaturase 1 Inhibition | journal = Journal of Breast Cancer | volume = 17 | issue = 2 | pages = 136–42 | date = Jun 2014 | pmid = 25013434 | pmc = 4090315 | doi = 10.4048/jbc.2014.17.2.136 }} 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 SREBP-1c-dependent mechanism. Activation of SREBP-1c results in upregulated synthesis of MUFAs and liver triglycerides. SCD-1 knockout mice did not increase de novo lipogenesis but created an abundance of cholesterol esters.{{Cite journal|last1=Flowers|first1=Matthew T.|last2=Groen|first2=Albert K.|last3=Oler|first3=Angie Tebon|last4=Keller|first4=Mark P.|last5=Choi|first5=Younjeong|last6=Schueler|first6=Kathryn L.|last7=Richards|first7=Oliver C.|last8=Lan|first8=Hong|last9=Miyazaki|first9=Makoto|date=2006-12-01|title=Cholestasis and hypercholesterolemia in SCD1-deficient mice fed a low-fat, high-carbohydrate diet|journal=Journal of Lipid Research|volume=47|issue=12|pages=2668–2680|doi=10.1194/jlr.M600203-JLR200|issn=0022-2275|pmid=17005996|doi-access=free}}

SCD1 function has also been shown to be involved in germ cell determination,{{cite journal | vauthors = Ben-David U, Gan QF, Golan-Lev T, Arora P, Yanuka O, Oren YS, Leikin-Frenkel A, Graf M, Garippa R, Boehringer M, Gromo G, Benvenisty N | title = Selective elimination of human pluripotent stem cells by an oleate synthesis inhibitor discovered in a high-throughput screen | journal = Cell Stem Cell | volume = 12 | issue = 2 | pages = 167–79 | date = Feb 2013 | pmid = 23318055 | doi = 10.1016/j.stem.2012.11.015 | doi-access = free }} adipose tissue specification, liver cell differentiation{{cite journal | vauthors = Rahimi Y, Mehdizadeh A, Nozad Charoudeh H, Nouri M, Valaei K, Fayezi S, Darabi M | title = Hepatocyte differentiation of human induced pluripotent stem cells is modulated by stearoyl-CoA desaturase 1 activity | journal = Development, Growth & Differentiation | date = Dec 2015 | pmid = 26676854 | doi = 10.1111/dgd.12255 | volume=57 | issue = 9 | pages=667–74| doi-access = free }} and cardiac development.{{cite journal | vauthors = Zhang L, Pan Y, Qin G, Chen L, Chatterjee TK, Weintraub NL, Tang Y | title = Inhibition of stearoyl-coA desaturase selectively eliminates tumorigenic Nanog-positive cells: improving the safety of iPS cell transplantation to myocardium | journal = Cell Cycle | volume = 13 | issue = 5 | pages = 762–71 | year = 2014 | pmid = 24394703 | doi = 10.4161/cc.27677 | pmc=3979912}}

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 hypertriglyceridemia, atherosclerosis, and diabetes.{{Cite journal|last1=Mar-Heyming|first1=Rebecca|last2=Miyazaki|first2=Makoto|last3=Weissglas-Volkov|first3=Daphna|last4=Kolaitis|first4=Nicholas A.|last5=Sadaat|first5=Narimaan|last6=Plaisier|first6=Christopher|last7=Pajukanta|first7=Päivi|last8=Cantor|first8=Rita M.|last9=de Bruin|first9=Tjerk W. A.|date=2008-06-01|title=Association of stearoyl-CoA desaturase 1 activity with familial combined hyperlipidemia|journal=Arteriosclerosis, Thrombosis, and Vascular Biology|volume=28|issue=6|pages=1193–1199|doi=10.1161/ATVBAHA.107.160150|issn=1524-4636|pmc=2758768|pmid=18340007}} One study showed that SCD-1 activity was associated with inherited hyperlipidemia. SCD-1 deficiency has also been shown to reduce ceramide synthesis by downregulating serine palmitoyltransferase. This consequently increases the rate of beta-oxidation in skeletal muscle.{{Cite book|title=Stearoyl-CoA Desaturase Genes in Lipid Metabolism|last1=Dobrzyn|first1=Pawel|last2=Dobrzyn|first2=Agnieszka|date=2013-01-01|publisher=Springer New York|isbn=9781461479680|editor-last=Ntambi|editor-first=James M.|pages=85–101|language=en|doi=10.1007/978-1-4614-7969-7_8}}

In carbohydrate metabolism studies, knockout SCD-1 mice show increased insulin sensitivity. Oleate is a major constituent of membrane phospholipids and membrane fluidity is influenced by the ratio of saturated to monounsaturated fatty acids.{{Cite journal|last1=Rahman|first1=Shaikh Mizanoor|last2=Dobrzyn|first2=Agnieszka|last3=Dobrzyn|first3=Pawel|last4=Lee|first4=Seong-Ho|last5=Miyazaki|first5=Makoto|last6=Ntambi|first6=James M.|date=2003-09-16|title=Stearoyl-CoA desaturase 1 deficiency elevates insulin-signaling components and down-regulates protein-tyrosine phosphatase 1B in muscle|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=100|issue=19|pages=11110–11115|doi=10.1073/pnas.1934571100|issn=0027-8424|pmc=196935|pmid=12960377|bibcode=2003PNAS..10011110R|doi-access=free}} One proposed mechanism is that an increase in cell membrane fluidity, consisting largely of lipid, activates the insulin receptor. 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.{{Cite journal|last1=Hagen|first1=Rachel M.|last2=Rodriguez-Cuenca|first2=Sergio|last3=Vidal-Puig|first3=Antonio|date=2010-06-18|title=An allostatic control of membrane lipid composition by SREBP1|journal=FEBS Letters|series=Gothenburg Special Issue: Molecules of Life|volume=584|issue=12|pages=2689–2698|doi=10.1016/j.febslet.2010.04.004|pmid=20385130|s2cid=10699298|doi-access=}}

• Cyclopropene acid
• Fatty acid desaturase
• Fatty acid synthesis

{{reflist|1}}

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{{refbegin|33em}}

• {{cite journal | vauthors = Mziaut H, Korza G, Ozols J | title = The N terminus of microsomal Δ 9 stearoyl-CoA desaturase contains the sequence determinant for its rapid degradation | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 16 | pages = 8883–8 | date = Aug 2000 | pmid = 10922050 | pmc = 16790 | doi = 10.1073/pnas.97.16.8883 | doi-access = free }}
• {{cite journal | vauthors = Samuel W, Kutty RK, Nagineni S, Gordon JS, Prouty SM, Chandraratna RA, Wiggert B | title = Regulation of stearoyl coenzyme A desaturase expression in human retinal pigment epithelial cells by retinoic acid | journal = The Journal of Biological Chemistry | volume = 276 | issue = 31 | pages = 28744–50 | date = Aug 2001 | pmid = 11397803 | doi = 10.1074/jbc.M103587200 | doi-access =free }}
• {{cite journal | vauthors = Zhang L, Ge L, Tran T, Stenn K, Prouty SM | title = Isolation and characterization of the human stearoyl-CoA desaturase gene promoter: requirement of a conserved CCAAT cis-element | journal = The Biochemical Journal | volume = 357 | issue = Pt 1 | pages = 183–93 | date = Jul 2001 | pmid = 11415448 | pmc = 1221940 | doi = 10.1042/0264-6021:3570183 }}
• {{cite journal | vauthors = Samuel W, Nagineni CN, Kutty RK, Parks WT, Gordon JS, Prouty SM, Hooks JJ, Wiggert B | title = Transforming growth factor-beta regulates stearoyl coenzyme A desaturase expression through a Smad signaling pathway | journal = The Journal of Biological Chemistry | volume = 277 | issue = 1 | pages = 59–66 | date = Jan 2002 | pmid = 11677241 | doi = 10.1074/jbc.M108730200 | doi-access = free }}
• {{cite journal | vauthors = Choi Y, Park Y, Storkson JM, Pariza MW, Ntambi JM | title = 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 | journal = Biochemical and Biophysical Research Communications | volume = 294 | issue = 4 | pages = 785–90 | date = Jun 2002 | pmid = 12061775 | doi = 10.1016/S0006-291X(02)00554-5 }}
• {{cite journal | vauthors = Attie AD, Krauss RM, Gray-Keller MP, Brownlie A, Miyazaki M, Kastelein JJ, Lusis AJ, Stalenhoef AF, Stoehr JP, Hayden MR, Ntambi JM | title = Relationship between stearoyl-CoA desaturase activity and plasma triglycerides in human and mouse hypertriglyceridemia | journal = Journal of Lipid Research | volume = 43 | issue = 11 | pages = 1899–907 | date = Nov 2002 | pmid = 12401889 | doi = 10.1194/jlr.M200189-JLR200 | doi-access = free | hdl = 2066/185468 | hdl-access = free }}
• {{cite journal | vauthors = Cohen P, Ntambi JM, Friedman JM | title = Stearoyl-CoA desaturase-1 and the metabolic syndrome | journal = Current Drug Targets. Immune, Endocrine and Metabolic Disorders | volume = 3 | issue = 4 | pages = 271–80 | date = Dec 2003 | pmid = 14683458 | doi = 10.2174/1568008033340117 }}
• {{cite journal | vauthors = Shiwaku K, Hashimoto M, Kitajima K, Nogi A, Anuurad E, Enkhmaa B, Kim JM, Kim IS, Lee SK, Oyunsuren T, Shido O, Yamane Y | title = Triglyceride levels are ethnic-specifically associated with an index of stearoyl-CoA desaturase activity and n-3 PUFA levels in Asians | journal = Journal of Lipid Research | volume = 45 | issue = 5 | pages = 914–22 | date = May 2004 | pmid = 14967817 | doi = 10.1194/jlr.M300483-JLR200 | doi-access = free }}
• {{cite journal | vauthors = Wang Y, Kurdi-Haidar B, Oram JF | title = LXR-mediated activation of macrophage stearoyl-CoA desaturase generates unsaturated fatty acids that destabilize ABCA1 | journal = Journal of Lipid Research | volume = 45 | issue = 5 | pages = 972–80 | date = May 2004 | pmid = 14967823 | doi = 10.1194/jlr.M400011-JLR200 | doi-access = free }}
• {{cite journal | vauthors = Rahman SM, Dobrzyn A, Dobrzyn P, Lee SH, Miyazaki M, Ntambi JM | title = Stearoyl-CoA desaturase 1 deficiency elevates insulin-signaling components and down-regulates protein-tyrosine phosphatase 1B in muscle | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 100 | issue = 19 | pages = 11110–5 | date = Sep 2003 | pmid = 12960377 | pmc = 196935 | doi = 10.1073/pnas.1934571100 | bibcode = 2003PNAS..10011110R | doi-access = free }}

{{refend}}

• {{MeshName|Stearoyl-CoA+Desaturase}}

{{Dioxygenases}}

{{Enzymes}}

{{Portal bar|Biology|border=no}}

Category:EC 1.14.19

Category:Iron enzymes

Category:Enzymes of unknown structure