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Black PN, DiRusso CC. Transmembrane movement of exogenous long-chain fatty acids: proteins, enzymes, and vectorial esterification. Microbiol Mol Biol Rev 2004; 67:454-472. A comprehensive review of the roles of FATP and ACS in transmembrane fatty acid transport coupled to activation of acyl-CoA, drawing on the data gathered from bacterial and yeast model systems.
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Hall AM, Smith AJ, Bernlohr DA. Characterization of the acyl-CoA synthetase activity of purified murine fatty acid transport protein 1. J Biol Chem 2003; 278:43008-43013. This article provides a clear demonstration that purified FATP1 has intrinsic ACS activity with a broad specificity for both LCFAs and VLCFAs. Interestingly, FATP1 is a low velocity enzyme compared with ACS1 and is not inhibited by Triacsin C, a potent competitive inhibitor of ACS1, suggesting nonoverlapping roles for FATP1 and ACS1.
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