Fatty acid synthase

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	== Relevance ==		== Relevance ==
-	FAS is as target of anti-cancer drugs.	+	FAS is as target of anti-cancer drugs. FAS from Mycobacterium tuberculosis inhibitors are possible anti-tuberculosis drugs<ref>PMID:30150274</ref> .
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	== Structural insights ==		== Structural insights ==

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Revision as of 08:04, 27 June 2019

spinqualitylabelsall models Human FAS thioesterase domain complex with fatty acid (PDB code 3tjm) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural insights 4 3D structures of fatty acid synthase Function Fatty acid synthase (FAS) catalizes the synthesis of palmitate from acetyl CoA and malonyl CoA into long chain fatty acid[1] . FAS is a multi-domain enzyme. It contains an acyl carrier protein domain (ACP). Relevance FAS is as target of anti-cancer drugs. FAS from Mycobacterium tuberculosis inhibitors are possible anti-tuberculosis drugs[2] . Structural insights (Hydrophobic, Polar). The [3]. 3D structures of fatty acid synthase Fatty acid synthase 3D structures

References

1. ↑ Smith S, Witkowski A, Joshi AK. Structural and functional organization of the animal fatty acid synthase. Prog Lipid Res. 2003 Jul;42(4):289-317. PMID:12689621
2. ↑ Edwards TJ, Marsh APL, Lockhart PJ, Richards LJ, Leventer RJ. Teaching NeuroImages: Imaging features of DCC-mediated mirror movements and isolated agenesis of the corpus callosum. Neurology. 2018 Aug 28;91(9):e886-e887. doi: 10.1212/WNL.0000000000006085. PMID:30150274 doi:http://dx.doi.org/10.1212/WNL.0000000000006085
3. ↑ Zhang W, Chakravarty B, Zheng F, Gu Z, Wu H, Mao J, Wakil SJ, Quiocho FA. Crystal structure of FAS thioesterase domain with polyunsaturated fatty acyl adduct and inhibition by dihomo-{gamma}-linolenic acid. Proc Natl Acad Sci U S A. 2011 Sep 20;108(38):15757-62. Epub 2011 Sep 9. PMID:21908709 doi:10.1073/pnas.1112334108