The Structure of Mammalian Fatty Acid Synthase Turned Back to Front
Author:
Publisher
Elsevier BV
Subject
Clinical Biochemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,General Medicine,Biochemistry
Reference16 articles.
1. Head-to-Head Coiled Arrangement of the Subunits of the Animal Fatty Acid Synthase
2. Mammalian Fatty Acid Synthase
3. Structural and functional organization of the animal fatty acid synthase
4. Animal fatty acid synthetase. A novel arrangement of the beta-ketoacyl synthetase sites comprising domains of the two subunits.
5. The arrangement and role of some of the amino acid residues in the beta-ketoacyl synthetase site of chicken liver fatty acid synthetase.
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2. Novel Structural Components Contribute to the High Thermal Stability of Acyl Carrier Protein from Enterococcus faecalis;Journal of Biological Chemistry;2016-01
3. The chain-flipping mechanism of ACP (acyl carrier protein)-dependent enzymes appears universal;Biochemical Journal;2014-05-13
4. Inefficient Translation Renders the Enterococcus faecalis fabK Enoyl-Acyl Carrier Protein Reductase Phenotypically Cryptic;Journal of Bacteriology;2013-10-25
5. Crystal Structures of Enoyl-ACP Reductases I (FabI) and III (FabL) from B. subtilis;Journal of Molecular Biology;2011-02
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