Stearoyl-coenzyme A desaturase

Terra22 ino S, Berto F, Carbonate MD, Fabris M, Guiotto A, Bernardini D, Leon A, Stearoylethanolamide exerts anorexic effects in mice via downregulation of liver stearoyl-coenzyme A desaturase-1 mRNA expression, FASEB / 18 1580— 1582, 2004. 

Strittmatter P., Spatz L., Corcoran D., Rogers M. J., Setlow B. and Redline R. (1974) Purification and properties of rat liver microsomal stearoyl coenzyme A desaturase. Proc. Natl. Acad. Sci. USA 71, 4565-4569. 

Thiede M. A., Ozols J. and Strittmatter P. (1986) Construction and sequence of cDNA for rat liver stearoyl coenzyme A desaturase. J. Biol. Chem. 261, 13230-13235. 

Terova, B., Petersen, G., Hansen, H. S., and Slotte, J. P. (2005). V-Acyl phosphatidylethanolamines affect the lateral distribution of cholesterol in membranes. Biochim. Biophys. Acta 1715, 49 56. Terrazzino, S., Berto, F., Carbonare, M. D., Fabris, M., Guiotto, A., Bernardini, D., and Leon, A. (2004). Stearoylethanolamide exerts anorexic effects in mice via down-regulation ofliver stearoyl-coenzyme A desaturase-1 mma expression. FASEBJ. 18, 1580-1582. 

Cameron, P.J., Rogers, M., Oman, J., May, S.G., Lunt, D.K., Smith, S.B. 1994. Stearoyl coenzyme A desaturase enzyme activity and mRNA levels are not different in subcutaneous adipose tissue from Angus and American Wagyu steers. J. Anim. Sci. 72, 2624-2628. 

Chu, K., Miyazaki, M., Man, W.M., Ntambi, J.M. 2006. Stearoyl-coenzyme A desaturase 1 deficiency protects against hypertriglyceridemia and increases plasma high-density lipoprotein cholesterol induced by liver X receptor activation. Mol. Cell. Biol. 26, 6786-6798. 

Busch, A.K., E. Gurislk, D.V. Cordery, M. Sudlow, G.S. Denyer, D.R. Laybutt, W.E. Hughes, T.J. Biden. Increased Fatty Acid Desatutation and Enhanced Expression of Stearoyl Coenzyme A Desaturase Protects Pancreatic P-Cells From Lipoapoptosis, Diabetes 54 2917-2924 (2005). 

Cooney, A., and Headon, D.R. (1989) Molecular Cloning of the Bovine Gene Encoding the Stearoyl Coenzyme A Desaturase, Biochem. Soc. Trans. 17,382 (Abstr.). 

Heinemann, F.S., and Ozols, J. (1998) Degradation of Stearoyl-Coenzyme A Desaturase Endoproteolytic Cleavage by an Integral Membrane Protease, Mol. Biol. 

Shang, X.G., Wang, F.L., Li, D.F., Yin, J.D., li, X.J., and Yi GJ., Effect of dietary conjugated linoleic acid on the fatty acid composition of egg yolk, plasma and Uver as well as hepatic stearoyl-coenzyme A desaturase activity and gene expression in laying hens. Poult. Sci., 84, 1886-1892, 2005. 

Flowers, M.T. Ntambi, J.M. Role of stearoyl-coenzyme A desaturase in regulating lipid metabohsm. Curr. Opin. Lipidol. 2008,19, 248-256. 

The endoplasmic reticulum is a site for the introduction of double bonds ( desaturation ) into fatty acids. The pathway used is almost universal, having been identified in bacteria, yeasts, algae, higher plants, protozoa and animals. Examples are the conversion of stearic acid (18 0) to oleic acid (18 ln-9) and of palmitic acid (16 0) to palmitoleic acid (16 ln-7) by the insertion of a cis double bond between carbons 9 and 10. Because the double bond is inserted between carbons 9 and 10 counting from the carboxyl end of the acyl chain, the desaturase enzyme is known as delta-9 desaturase (A -desaturase), although sometimes this enzyme is referred to as stearoyl CoA (coenzyme A) desaturase. 

Fatty acid synthase (FAS) constitutes a multisubunit complex in the plastid where it catalyzes ordered synthesis of fatty acids, initiated from acetyl CoA and malonyl CoA [146, 147]. Stepwise FAS activity generates the products 16 0-acyl carrier protein (AGP) and 18 0-ACP. Most of the 18 0-ACP is desaturated by a soluble stearoyl-ACP desaturase, yielding 18 1 D9-ACP [148]. Acyl-ACP thioesterases release AGP from 16 0-AGP and 18 0-AGP the deacylated fatty acids exit the plastid and are then esterified with coenzyme A (GoA) to form respective acyl-GoAs [148]. These acyl moieties are then esterified to phosphatidylcholine (PQ and then undergo desaturation by D12- and D15-desaturases to yield the essential fatty acids, linoleic acid, and a-linolenic acid [148-150], All higher plants have the enzymes for synthesizing the G18 PUFAs linoleic acid and a-linolenic acid. The primary genes involved in PUFA biosynthesis have been reviewed [151],... 

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