Crystal structure of FAS thioesterase domain with polyunsaturated fatty acyl adduct and inhibition by dihomo-γ-linolenic acid

Human fatty acid synthase (hFAS) is a homodimeric multidomain enzyme that catalyzes a series of reactions leading to the de novo biosynthesis of long-chain fatty acids, mainly palmitate. The carboxy-terminal thioesterase (TE) domain determines the length of the fatty acyl chain and its ultimate rele...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2011-09, Vol.108 (38), p.15757-15762
Hauptverfasser:	Zhang, Wei, Chakravarty, Bornali, Zheng, Fei, Gu, Ziwei, Wu, Hongmei, Mao, Jianqiang, Wakil, Salih J, Quiocho, Florante A
Format:	Artikel
Sprache:	eng
Schlagworte:	3T3-L1 Cells 8,11,14-Eicosatrienoic Acid - pharmacology Active sites Adipocytes - drug effects Adipocytes - metabolism alpha-linolenic acid alpha-Linolenic Acid - pharmacology Animals Biocatalysis - drug effects Biological Sciences Biosynthesis Breast cancer breast neoplasms Cancer Catalytic Domain Cell Line, Tumor Cell lines Crystal structure Crystallization Crystallography, X-Ray diabetes Esters Fatty Acid Synthases - chemistry Fatty Acid Synthases - metabolism Fatty acids Fatty Acids - biosynthesis Fatty Acids, Unsaturated - chemistry Fatty Acids, Unsaturated - metabolism fatty-acid synthase heart diseases Humans hydrolysis long chain polyunsaturated fatty acids Mice Models, Molecular Molecular Structure Palmitates phosphorylation Protein Binding - drug effects Protein Structure, Tertiary serine therapeutics Thiolester Hydrolases - chemistry Thiolester Hydrolases - metabolism Unsaturated fatty acids
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