Fatty acid synthase
From Proteopedia
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| + | == Function == | ||
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'''Fatty acid synthase''' (FAS) catalizes the synthesis of palmitate from acetyl CoA and malonyl CoA into long chain fatty acid<ref>PMID:12689621</ref> . FAS is a multi-domain enzyme. It contains an acyl carrier protein domain (ACP). | '''Fatty acid synthase''' (FAS) catalizes the synthesis of palmitate from acetyl CoA and malonyl CoA into long chain fatty acid<ref>PMID:12689621</ref> . FAS is a multi-domain enzyme. It contains an acyl carrier protein domain (ACP). | ||
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| + | == Relevance == | ||
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| + | FAS is as target of anti-cancer drugs. | ||
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| + | == Structural insights == | ||
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| + | The long fatty acid ligand is nestled in a long groove and tunnel<ref>PMID:21908709</ref>. | ||
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</StructureSection> | </StructureSection> | ||
Revision as of 15:38, 21 January 2016
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3D structures of fatty acid synthase
Updated on 21-January-2016
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
- ↑ 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
