Structural basis for different specificities of acyltransferases associated with the human cytosolic and mitochondrial fatty acid synthases.

Journal article

Animals employ two systems for the de novo biosynthesis of fatty acids: a megasynthase complex in the cytosol (type I) that produces mainly palmitate, and an ensemble of freestanding enzymes in the mitochondria (type II) that produces mainly octanoyl moieties. The acyltransferases responsible for initiation of fatty acid biosynthesis in the two compartments are distinguished by their different substrate specificities: the type I enzyme transfers both the acetyl primer and the malonyl chain ex...

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Authors: Bunkoczi, G; Misquitta, S; Wu, X; Lee, W; Rojkova, A

• Publication status: Published
• Journal: Chemistry and biology
• Volume: 16
• Issue: 6
• Pages: 667-675
• Publication date: 2009-06-01
• DOI: 10.1016/j.chembiol.2009.04.011
• EISSN: 1879-1301
• ISSN: 1074-5521
• Language: English
• Keywords: Amino Acid Sequence; Molecular Sequence Data; Sequence Homology, Amino Acid; Cytosol; Fatty Acid Synthase, Type I; Computer Simulation; Catalytic Domain; Crystallography, X-Ray; Sequence Alignment; Acyltransferases; Fatty Acids; Substrate Specificity; Mitochondria; Mutagenesis, Site-Directed; Mutant Proteins; Humans; Fatty Acid Synthase, Type II