Fatty acid synthase

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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 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. Structural insights (Hydrophobic, Polar). The [2].

3D structures of fatty acid synthase

Updated on 17-March-2019

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. ↑ 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