SLC27A3 ligates CoA-SH to VLCFA

Stable Identifier
Reaction [transition]
Homo sapiens
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Acyl-coenzyme A synthetases catalyse the activation of fatty acids by thioesterification to CoA, the fundamental initial reaction in fatty acid oxidation. Members of the long chain acyl-coenzyme A synthetases (ACSVL) subfamily were originally thought to be fatty acid transport proteins (FATPs), hence their approved gene names and symbols are “solute carrier family 27 (fatty acid transporter) member x" (SLC27Ax) but their transport function has never been proven. Instead, their amino acid sequence contains two highly conserved motifs characteristic of acyl-CoA synthetases. Long-chain fatty acid transport protein 3 (SLC27A3, aka ACSVL3, FATP3) preferentially ligates CoA-SH to very long-chain fatty acids (VLCFA) (Watkins et al. 2007). The activity of human SLC27A3 is inferred from mouse Slc27a3 functional studies (Pei et al. 2004).
Literature References
PubMed ID Title Journal Year
15469937 Mouse very long-chain Acyl-CoA synthetase 3/fatty acid transport protein 3 catalyzes fatty acid activation but not fatty acid transport in MA-10 cells

Berger, J, Watkins, PA, Jia, Z, Pei, Z, Fraisl, P, Forss-Petter, S

J. Biol. Chem. 2004
17762044 Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome

Pevsner, J, Jia, Z, Watkins, PA, Maiguel, D

J. Lipid Res. 2007
Catalyst Activity

very long-chain fatty acid-CoA ligase activity of SLC27A3 [mitochondrial matrix]

Inferred From
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