Fatty acid synthase

From Proteopedia

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). See also Lipid metabolism.

Relevance

FAS is as target of anti-cancer drugs. FAS from Mycobacterium tuberculosis inhibitors are possible anti-tuberculosis drugs^[2] .

Structural insights

Active site predominantly consists of hydrophobic/non-polar residues (Hydrophobic, Polar). The long fatty acid ligand is nestled in a long groove and tunnel^[3].

3D structures of fatty acid synthase

Fatty acid synthase 3D structures

Human FAS thioesterase domain complex with fatty acid (PDB code 3tjm)

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References

↑ 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
↑ Elad N, Baron S, Peleg Y, Albeck S, Grunwald J, Raviv G, Shakked Z, Zimhony O, Diskin R. Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 A resolution. Nat Commun. 2018 Sep 24;9(1):3886. doi: 10.1038/s41467-018-06440-6. PMID:30250274 doi:http://dx.doi.org/10.1038/s41467-018-06440-6
↑ 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