Characterization of the Acyl-CoA Synthetase Activity of Purified Murine Fatty Acid Transport Protein 1 *
作者： Angela M. Hall , Anne J. Smith , David A. Bernlohr
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摘要: Fatty acid transport protein 1 (FATP1) is an ∼63-kDa plasma membrane that facilitates the influx of fatty acids into adipocytes as well skeletal and cardiac myocytes. Previous studies with FATP1 expressed in COS1 cell extracts suggested exhibits very long chain acyl-CoA synthetase (ACS) activity such may be linked to transport. To address enzymatic isolated protein, murine ACS1 were engineered contain a C-terminal Myc-His tag cells via adenoviral-mediated infection purified homogeneity using nickel affinity chromatography. Kinetic analysis enzymes was carried out for palmitic (C16:0) lignoceric (C24:0) ATP CoA. exhibited similar substrate specificity 16–24 carbons length, whereas 10-fold more active on relative acids. The two comparable Km values both coenzyme A. Interestingly, insensitive inhibition by triacsin C, inhibited micromolar concentrations compound. These data represent first characterization indicate enzyme broad synthetase. findings are consistent hypothesis uptake their esterification
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