- Stearoyl-CoA desaturase-1
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Stearoyl-CoA desaturase (delta-9-desaturase) Identifiers Symbols SCD; FADS5; MSTP008; SCD1; SCDOS External IDs OMIM: 604031 HomoloGene: 74538 GeneCards: SCD Gene EC number 1.14.19.1 Gene Ontology Molecular function • stearoyl-CoA 9-desaturase activity
• iron ion binding
• oxidoreductase activity
• oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of waterCellular component • endoplasmic reticulum
• endoplasmic reticulum membrane
• membrane
• integral to membraneBiological process • fatty acid biosynthetic process Sources: Amigo / QuickGO Orthologs Species Human Mouse Entrez 6319 20249 Ensembl ENSG00000099194 ENSMUSG00000037071 UniProt O00767 P13516 RefSeq (mRNA) NM_005063.4 NM_009127.4 RefSeq (protein) NP_005054.3 NP_033153.2 Location (UCSC) Chr 10:
102.11 – 102.12 MbChr 19:
44.47 – 44.48 MbPubMed search [1] [2] This box: view · protein that in humans is encoded by the SCD gene.[1] Stearoyl-CoA desaturase-1is a key enzyme in fatty acid metabolism. It is responsible for forming a double bond in Stearoyl-CoA. This is how the monounsaturated fatty acid oleic acid is produced from the saturated fatty acid stearic acid.
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. Four SCD isoforms, Scd1 through Scd4, have been identified in mouse. In contrast, only 2 SCD isoforms, SCD1 and SCD5 (MIM 608370), 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 shares limited homology with the rodent SCDs and appears to be unique to primates.[2][3][1]
References
- ^ a b "Entrez Gene: Stearoyl-CoA desaturase (delta-9-desaturase)". http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&list_uids=6319. Retrieved 2011-09-29T21:11:57.607-07:00.
- ^ Zhang, L.; Ge, L.; Parimoo, S.; Stenn, K.; Prouty, S. M. (1999). "Human stearoyl-CoA desaturase: Alternative transcripts generated from a single gene by usage of tandem polyadenylation sites". The Biochemical journal 340 ( Pt 1) (Pt 1): 255–264. PMC 1220244. PMID 10229681. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1220244. edit
- ^ Wang J, Yu L, Schmidt RE, Su C, Huang X, Gould K, Cao G (July 2005). "Characterization of HSCD5, a novel human stearoyl-CoA desaturase unique to primates". Biochem. Biophys. Res. Commun. 332 (3): 735–42. doi:10.1016/j.bbrc.2005.05.013. PMID 15907797.
Further reading
- Zhang, L.; Ge, L.; Parimoo, S.; Stenn, K.; Prouty, S. M. (1999). "Human stearoyl-CoA desaturase: Alternative transcripts generated from a single gene by usage of tandem polyadenylation sites". The Biochemical journal 340 ( Pt 1) (Pt 1): 255–264. PMC 1220244. PMID 10229681. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1220244. edit
- Mziaut, H.; Korza, G.; Ozols, J. (2000). "The N terminus of microsomal Δ9 stearoyl-CoA desaturase contains the sequence determinant for its rapid degradation". Proceedings of the National Academy of Sciences of the United States of America 97 (16): 8883–8888. PMC 16790. PMID 10922050. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16790. edit
- Samuel, W.; Kutty, R. K.; Nagineni, S.; Gordon, J. S.; Prouty, S. M.; Chandraratna, R. A.; Wiggert, B. (2001). "Regulation of Stearoyl Coenzyme a Desaturase Expression in Human Retinal Pigment Epithelial Cells by Retinoic Acid". Journal of Biological Chemistry 276 (31): 28744–28750. doi:10.1074/jbc.M103587200. PMID 11397803. edit
- Zhang, L.; Ge, L.; Tran, T.; Stenn, K.; Prouty, S. M. (2001). "Isolation and characterization of the human stearoyl-CoA desaturase gene promoter: Requirement of a conserved CCAAT cis-element". The Biochemical journal 357 (Pt 1): 183–193. PMC 1221940. PMID 11415448. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1221940. edit
- Samuel, W.; Nagineni, C. N.; Kutty, R. K.; Parks, W. T.; Gordon, J. S.; Prouty, S. M.; Hooks, J. J.; Wiggert, B. (2001). "Transforming Growth Factor-beta Regulates Stearoyl Coenzyme a Desaturase Expression through a Smad Signaling Pathway". Journal of Biological Chemistry 277 (1): 59–66. doi:10.1074/jbc.M108730200. PMID 11677241. edit
- Choi, Y.; Park, Y.; Storkson, J. M.; Pariza, M. W.; Ntambi, J. M. (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". Biochemical and Biophysical Research Communications 294 (4): 785–790. doi:10.1016/S0006-291X(02)00554-5. PMID 12061775. edit
- Attie, A. D.; Krauss, R. M.; Gray-Keller, M. P.; Brownlie, A.; Miyazaki, M.; Kastelein, J. J.; Lusis, A. J.; Stalenhoef, A. F. et al. (2002). "Relationship between stearoyl-CoA desaturase activity and plasma triglycerides in human and mouse hypertriglyceridemia". Journal of lipid research 43 (11): 1899–1907. PMID 12401889. edit
- Cohen, P.; Ntambi, J. M.; Friedman, J. M. (2003). "Stearoyl-CoA desaturase-1 and the metabolic syndrome". Current drug targets. Immune, endocrine and metabolic disorders 3 (4): 271–280. PMID 14683458. edit
- Shiwaku, K.; Hashimoto, M.; Kitajima, K.; Nogi, A.; Anuurad, E.; Enkhmaa, B.; Kim, J. M.; Kim, I. S. et al. (2004). "Triglyceride levels are ethnic-specifically associated with an index of stearoyl-CoA desaturase activity and n-3 PUFA levels in Asians". The Journal of Lipid Research 45 (5): 914–922. doi:10.1194/jlr.M300483-JLR200. PMID 14967817. edit
- Wang, Y.; Kurdi-Haidar, B.; Oram, J. F. (2004). "LXR-mediated activation of macrophage stearoyl-CoA desaturase generates unsaturated fatty acids that destabilize ABCA1". The Journal of Lipid Research 45 (5): 972–980. doi:10.1194/jlr.M400011-JLR200. PMID 14967823. edit
- Rahman SM, Dobrzyn A, Dobrzyn P et al. (2003). "Stearoyl-CoA desaturase 1 deficiency elevates insulin-signaling components and down-regulates protein-tyrosine phosphatase 1B in muscle". Proc. Natl. Acad. Sci. U.S.A. 100 (19): 11110–5. doi:10.1073/pnas.1934571100. PMC 196935. PMID 12960377. http://www.pnas.org/cgi/content/abstract/100/19/11110.
External links
v · d · eOxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14) 1.14.11: 2-oxoglutarate 1.14.13: NADH or NADPH Flavin-containing monooxygenase (FMO1, FMO2, FMO3, FMO4, FMO5) - Nitric oxide synthase (NOS1, NOS2, NOS3) - Cholesterol 7 alpha-hydroxylase - Methane monooxygenase - 3A4 - Lanosterol 14 alpha-demethylase1.14.14: reduced flavin or flavoprotein 1.14.15: reduced iron-sulfur protein 1.14.16: reduced pteridine (BH4 dependent) 1.14.17: reduced ascorbate 1.14.18-19: other Tyrosinase - Stearoyl-CoA desaturase-11.14.99 - miscellaneous B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6 Categories:- Human proteins
- Oxidoreductase stubs
- Chromosome 10 gene stubs
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Stearoyl-CoA desaturase-1
- Stearoyl-CoA desaturase-1
-
Stearoyl-CoA desaturase (delta-9-desaturase) Identifiers Symbols SCD; FADS5; MSTP008; SCD1; SCDOS External IDs OMIM: 604031 HomoloGene: 74538 GeneCards: SCD Gene EC number 1.14.19.1 Gene Ontology Molecular function • stearoyl-CoA 9-desaturase activity
• iron ion binding
• oxidoreductase activity
• oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of waterCellular component • endoplasmic reticulum
• endoplasmic reticulum membrane
• membrane
• integral to membraneBiological process • fatty acid biosynthetic process Sources: Amigo / QuickGO Orthologs Species Human Mouse Entrez 6319 20249 Ensembl ENSG00000099194 ENSMUSG00000037071 UniProt O00767 P13516 RefSeq (mRNA) NM_005063.4 NM_009127.4 RefSeq (protein) NP_005054.3 NP_033153.2 Location (UCSC) Chr 10:
102.11 – 102.12 MbChr 19:
44.47 – 44.48 MbPubMed search [1] [2]